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The original isolate carried the MNR mutations S68G, V75I, F77L, F116Y and Q151M, the lamivudine mutation M184V, the NNRTI mutation K103N and the yet unreported K70S. After in vitro culturing in the absence of tenofovir, the virus acquired phenotypic resistance towards tenofovir, associated with the acquisition of K70T and the loss of M184V. These changes resulted in higher resistance levels towards zalcitabine, didanosine and tenofovir but lower levels towards zidovudine, stavudine and lamivudine. In vitro culturing in the presence of tenofovir resulted in further enhancement of phenotypic resistance levels towards tenofovir and nucleoside reverse transcriptase inhibitors due to the development of K65R. #","publication_date":"2007,,","publication_name":"Infection, Genetics and Evolution","grobid_abstract_attachment_id":"49012142"},"document_type":"paper","pre_hit_view_count_baseline":null,"quality":"high","language":"en","title":"Mutations at 65 and 70 within the context of a Q151M cluster in human immunodeficiency virus type 1 reverse transcriptase impact the susceptibility to the different nucleoside reverse transcriptase inhibitors in distinct ways","broadcastable":true,"draft":null,"has_indexable_attachment":true,"indexable":true}}["work"]; window.loswp.workCoauthors = [32636531]; window.loswp.locale = "en"; window.loswp.countryCode = "SG"; window.loswp.cwvAbTestBucket = ""; window.loswp.designVariant = "ds_vanilla"; window.loswp.fullPageMobileSutdModalVariant = "full_page_mobile_sutd_modal"; window.loswp.useOptimizedScribd4genScript = false; window.loginModal = {}; window.loginModal.appleClientId = 'edu.academia.applesignon';</script><script defer="" src="https://accounts.google.com/gsi/client"></script><div class="ds-loswp-container"><div class="ds-work-card--grid-container"><div class="ds-work-card--container js-loswp-work-card"><div class="ds-work-card--cover"><div class="ds-work-cover--wrapper"><div class="ds-work-cover--container"><button class="ds-work-cover--clickable js-swp-download-button" data-signup-modal="{"location":"swp-splash-paper-cover","attachmentId":49012142,"attachmentType":"pdf"}"><img alt="First page of “Mutations at 65 and 70 within the context of a Q151M cluster in human immunodeficiency virus type 1 reverse transcriptase impact the susceptibility to the different nucleoside reverse transcriptase inhibitors in distinct ways”" class="ds-work-cover--cover-thumbnail" src="https://0.academia-photos.com/attachment_thumbnails/49012142/mini_magick20190201-14330-86ns1q.png?1549081358" /><img alt="PDF Icon" class="ds-work-cover--file-icon" src="//a.academia-assets.com/images/single_work_splash/adobe_icon.svg" /><div class="ds-work-cover--hover-container"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span><p>Download Free PDF</p></div><div class="ds-work-cover--ribbon-container">Download Free PDF</div><div class="ds-work-cover--ribbon-triangle"></div></button></div></div></div><div class="ds-work-card--work-information"><h1 class="ds-work-card--work-title">Mutations at 65 and 70 within the context of a Q151M cluster in human immunodeficiency virus type 1 reverse transcriptase impact the susceptibility to the different nucleoside reverse transcriptase inhibitors in distinct ways</h1><div class="ds-work-card--work-authors ds-work-card--detail"><a class="ds-work-card--author js-wsj-grid-card-author ds2-5-body-md ds2-5-body-link" data-author-id="32636531" href="https://independent.academia.edu/AnnemiekeVandamme"><img alt="Profile image of Anne-mieke Vandamme" class="ds-work-card--author-avatar" src="//a.academia-assets.com/images/s65_no_pic.png" />Anne-mieke Vandamme</a></div><div class="ds-work-card--detail"><p class="ds-work-card--detail ds2-5-body-sm">2007, Infection, Genetics and Evolution</p><div class="ds-work-card--work-metadata"><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">visibility</span><p class="ds2-5-body-sm" id="work-metadata-view-count">…</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">description</span><p class="ds2-5-body-sm">4 pages</p></div><div class="ds-work-card--work-metadata__stat"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">link</span><p class="ds2-5-body-sm">1 file</p></div></div><script>(async () => { const workId = 28642607; const worksViewsPath = "/v0/works/views?subdomain_param=api&work_ids%5B%5D=28642607"; const getWorkViews = async (workId) => { const response = await fetch(worksViewsPath); if (!response.ok) { throw new Error('Failed to load work views'); } const data = await response.json(); return data.views[workId]; }; // Get the view count for the work - we send this immediately rather than waiting for // the DOM to load, so it can be available as soon as possible (but without holding up // the backend or other resource requests, because it's a bit expensive and not critical). const viewCount = await getWorkViews(workId); const updateViewCount = (viewCount) => { try { const viewCountNumber = parseInt(viewCount, 10); if (viewCountNumber === 0) { // Remove the whole views element if there are zero views. document.getElementById('work-metadata-view-count')?.parentNode?.remove(); return; } const commaizedViewCount = viewCountNumber.toLocaleString(); const viewCountBody = document.getElementById('work-metadata-view-count'); if (!viewCountBody) { throw new Error('Failed to find work views element'); } viewCountBody.textContent = `${commaizedViewCount} views`; } catch (error) { // Remove the whole views element if there was some issue parsing. document.getElementById('work-metadata-view-count')?.parentNode?.remove(); throw new Error(`Failed to parse view count: ${viewCount}`, error); } }; // If the DOM is still loading, wait for it to be ready before updating the view count. if (document.readyState === "loading") { document.addEventListener('DOMContentLoaded', () => { updateViewCount(viewCount); }); // Otherwise, just update it immediately. } else { updateViewCount(viewCount); } })();</script></div><p class="ds-work-card--work-abstract ds-work-card--detail ds2-5-body-md">We report a multinucleoside resistant (MNR) HIV-1 strain that was susceptible towards tenofovir but acquired phenotypic resistance towards tenofovir during in vitro selective pressure both in the presence and in the absence of tenofovir. The original isolate carried the MNR mutations S68G, V75I, F77L, F116Y and Q151M, the lamivudine mutation M184V, the NNRTI mutation K103N and the yet unreported K70S. After in vitro culturing in the absence of tenofovir, the virus acquired phenotypic resistance towards tenofovir, associated with the acquisition of K70T and the loss of M184V. These changes resulted in higher resistance levels towards zalcitabine, didanosine and tenofovir but lower levels towards zidovudine, stavudine and lamivudine. In vitro culturing in the presence of tenofovir resulted in further enhancement of phenotypic resistance levels towards tenofovir and nucleoside reverse transcriptase inhibitors due to the development of K65R. #</p><div class="ds-work-card--button-container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--work-card","attachmentId":49012142,"attachmentType":"pdf","workUrl":"https://www.academia.edu/28642607/Mutations_at_65_and_70_within_the_context_of_a_Q151M_cluster_in_human_immunodeficiency_virus_type_1_reverse_transcriptase_impact_the_susceptibility_to_the_different_nucleoside_reverse_transcriptase_inhibitors_in_distinct_ways"}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--work-card","attachmentId":49012142,"attachmentType":"pdf","workUrl":"https://www.academia.edu/28642607/Mutations_at_65_and_70_within_the_context_of_a_Q151M_cluster_in_human_immunodeficiency_virus_type_1_reverse_transcriptase_impact_the_susceptibility_to_the_different_nucleoside_reverse_transcriptase_inhibitors_in_distinct_ways"}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div></div><div data-auto_select="false" data-client_id="331998490334-rsn3chp12mbkiqhl6e7lu2q0mlbu0f1b" data-doc_id="49012142" data-landing_url="https://www.academia.edu/28642607/Mutations_at_65_and_70_within_the_context_of_a_Q151M_cluster_in_human_immunodeficiency_virus_type_1_reverse_transcriptase_impact_the_susceptibility_to_the_different_nucleoside_reverse_transcriptase_inhibitors_in_distinct_ways" data-login_uri="https://www.academia.edu/registrations/google_one_tap" data-moment_callback="onGoogleOneTapEvent" id="g_id_onload"></div><div class="ds-top-related-works--grid-container"><div class="ds-related-content--container ds-top-related-works--container"><h2 class="ds-related-content--heading">Related papers</h2><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="0" data-entity-id="29876761" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/29876761/Multiple_Drug_Resistance_to_Nucleoside_Analogues_and_Nonnucleoside_Reverse_Transcriptase_Inhibitors_in_an_Efficiently_Replicating_Human_Immunodeficiency_Virus_Type_1_Patient_Strain">Multiple Drug Resistance to Nucleoside Analogues and Nonnucleoside Reverse Transcriptase Inhibitors in an Efficiently Replicating Human Immunodeficiency Virus Type 1 Patient Strain</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="56725943" href="https://independent.academia.edu/PhilippeHermans">Philippe Hermans</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Infectious Diseases, 1996</p><p class="ds-related-work--abstract ds2-5-body-sm">A human immunodeficiency virus type 1 (HIV-l)-seropositive patient was treated sequentially with the dideoxynucleoside (ddN) analogues zidovudine, didanosine, zalcitabine, stavudine, and lamivudine and the nonnucleoside HIV-l-specific reverse transcriptase inhibitor (NNRTI) loviride (a-APA). Accumulation of drug resistance mutations (mainly V75I, F77L, K103N, F116Y, Q151M, and M184V) eventually resulted in a strain that was genotypically and phenotypically resistant to all tested ddNs and the majority of NNRTIs. However, the multidrug-resistant virus retained wild type sensitivities to drugs such as foscarnet, phosphonomethoxyethyl adenine, dextran sulfate, JM3100, saquinavir, and NNRTI TSAO-m 3T. Drug-resistant isolates showed replication kinetics and infectivity in an in vitro peripheral blood mononuclear cell system similar to those of the wild type isolate from the same patient. The multi-ddN -resistant isolate was not eliminated in a competition culture with the wild type isolate. Sequential therapy did not prevent the appearance of multidrug-resistant virus with a conserved replication rate.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Multiple Drug Resistance to Nucleoside Analogues and Nonnucleoside Reverse Transcriptase Inhibitors in an Efficiently Replicating Human Immunodeficiency Virus Type 1 Patient Strain","attachmentId":50344003,"attachmentType":"pdf","work_url":"https://www.academia.edu/29876761/Multiple_Drug_Resistance_to_Nucleoside_Analogues_and_Nonnucleoside_Reverse_Transcriptase_Inhibitors_in_an_Efficiently_Replicating_Human_Immunodeficiency_Virus_Type_1_Patient_Strain","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/29876761/Multiple_Drug_Resistance_to_Nucleoside_Analogues_and_Nonnucleoside_Reverse_Transcriptase_Inhibitors_in_an_Efficiently_Replicating_Human_Immunodeficiency_Virus_Type_1_Patient_Strain"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="1" data-entity-id="13481923" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/13481923/Involvement_of_Novel_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Mutations_in_the_Regulation_of_Resistance_to_Nucleoside_Inhibitors">Involvement of Novel Human Immunodeficiency Virus Type 1 Reverse Transcriptase Mutations in the Regulation of Resistance to Nucleoside Inhibitors</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="32696329" href="https://unimi.academia.edu/AntonellaMonforte">Antonella Monforte</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Virology, 2006</p><p class="ds-related-work--abstract ds2-5-body-sm">We characterized 16 additional mutations in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) whose role in drug resistance is still unknown by analyzing 1,906 plasma-derived HIV-1 subtype B pol sequences from 551 drug-naïve patients and 1,355 nucleoside RT inhibitor (NRTI)-treated patients. Twelve mutations positively associated with NRTI treatment strongly correlated both in pairs and in clusters with known NRTI resistance mutations on divergent evolutionary pathways. In particular, T39A, K43E/Q, K122E, E203K, and H208Y clustered with the nucleoside analogue mutation 1 cluster (NAM1; M41L؉L210W؉T215Y). Their copresence in this cluster was associated with an increase in thymidine analogue resistance. Moreover, treatment failure in the presence of K43E, K122E, or H208Y was significantly associated with higher viremia and lower CD4 cell count. Differently, D218E clustered with the NAM2 pathway (D67N؉K70R؉K219Q؉T215F), and its presence in this cluster determined an increase in zidovudine resistance. In contrast, three mutations (V35I, I50V, and R83K) negatively associated with NRTI treatment showed negative correlations with NRTI resistance mutations and were associated with increased susceptibility to specific NRTIs. In particular, I50V negatively correlated with the lamivudine-selected mutation M184V and was associated with a decrease in M184V/lamivudine resistance, whereas R83K negatively correlated with both NAM1 and NAM2 clusters and was associated with a decrease in thymidine analogue resistance. Finally, the association pattern of the F214L polymorphism revealed its propensity for the NAM2 pathway and its strong negative association with the NAM1 pathway. Our study provides evidence of novel RT mutational patterns that regulate positively and/or negatively NRTI resistance and strongly suggests that other mutations beyond those currently known to confer resistance should be considered for improved prediction of clinical response to antiretroviral drugs.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Involvement of Novel Human Immunodeficiency Virus Type 1 Reverse Transcriptase Mutations in the Regulation of Resistance to Nucleoside Inhibitors","attachmentId":45289865,"attachmentType":"pdf","work_url":"https://www.academia.edu/13481923/Involvement_of_Novel_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Mutations_in_the_Regulation_of_Resistance_to_Nucleoside_Inhibitors","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/13481923/Involvement_of_Novel_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Mutations_in_the_Regulation_of_Resistance_to_Nucleoside_Inhibitors"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="2" data-entity-id="12738288" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/12738288/A_6_basepair_insert_in_the_reverse_transcriptase_gene_of_human_immunodeficiency_virus_type_1_confers_resistance_to_multiple_nucleoside_inhibitors">A 6-basepair insert in the reverse transcriptase gene of human immunodeficiency virus type 1 confers resistance to multiple nucleoside inhibitors</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="31773965" href="https://independent.academia.edu/RobertShafer">Robert Shafer</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Clinical Investigation, 1998</p><p class="ds-related-work--abstract ds2-5-body-sm">While many point mutations in the HIV-1 reverse transcriptase (RT) confer resistance to antiretroviral drugs, inserts or deletions in this gene have not been previously characterized. In this report, 14 RT inhibitor-treated patients were found to have HIV-1 strains possessing a 6-basepair insert between codons 69 and 70 of the RT gene. Known drug resistance mutations were also observed in these strains, with T215Y appearing in all strains. Genotypic analysis indicated that the inserts had substantial nucleotide variability that resulted in relatively restricted sets of amino acid sequences. Linkage of patients' treatment histories with longitudinal sequencing data showed that insert strains appeared during drug regimens containing ddI or ddC, with prior or concurrent AZT treatment. Drug susceptibility tests of recombinant patient isolates showed reduced susceptibility to nearly all nucleoside RT inhibitors. Sitedirected mutagenesis studies confirmed the role of the inserts alone in conferring reduced susceptibility to most RT inhibitors. The addition of AZT-associated drug resistance mutations further increased the range and magnitude of resistance. These results establish that inserts, like point mutations, are selected in vivo during antiretroviral therapy and provide resistance to multiple nucleoside analogs. ( J.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"A 6-basepair insert in the reverse transcriptase gene of human immunodeficiency virus type 1 confers resistance to multiple nucleoside inhibitors","attachmentId":45971605,"attachmentType":"pdf","work_url":"https://www.academia.edu/12738288/A_6_basepair_insert_in_the_reverse_transcriptase_gene_of_human_immunodeficiency_virus_type_1_confers_resistance_to_multiple_nucleoside_inhibitors","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/12738288/A_6_basepair_insert_in_the_reverse_transcriptase_gene_of_human_immunodeficiency_virus_type_1_confers_resistance_to_multiple_nucleoside_inhibitors"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="3" data-entity-id="12630105" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/12630105/Broad_nucleoside_analogue_resistance_implications_for_human_immunodeficiency_virus_type_1_reverse_transcriptase_mutations_at_codons_44_and_118">Broad nucleoside-analogue resistance implications for human immunodeficiency virus type 1 reverse-transcriptase mutations at codons 44 and 118</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="31597037" href="https://independent.academia.edu/MaurizioZazzi">Maurizio Zazzi</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Infectious …, 2002</p><p class="ds-related-work--abstract ds2-5-body-sm">Two large, independent human immunodeficiency virus type 1 resistance databases containing . 7700 reverse-transcriptase (RT) sequences were used to analyze the epidemiology of amino acid substitutions at codons 44 and 118, which confer moderate lamivudine resistance in the presence of zidovudine resistance. As expected, E44A/D and V118I mutations were strongly associated with M41L, D67N, L210W, and T215Y but also with other mutations, including K43E/N/Q, T69D, V75M, H208Y, R211K, and K219R. Both E44D and V118I were more frequently associated with stavudine and didanosine than with zidovudine and lamivudine treatment. However, selection of E44A/D and V118I was also detected in association with a switch to other nucleoside RT inhibitors, including zalcitabine and abacavir. Site-directed mutagenesis confirmed that 44D and 118I can decrease phenotypic susceptibility not only to lamivudine but also to most other nucleoside analogues, particularly stavudine and abacavir. Thus, substitutions at RT codons 44 and 118 have broad implications in nucleoside RT inhibitor resistance in the setting of several nucleoside-associated mutations.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Broad nucleoside-analogue resistance implications for human immunodeficiency virus type 1 reverse-transcriptase mutations at codons 44 and 118","attachmentId":46038999,"attachmentType":"pdf","work_url":"https://www.academia.edu/12630105/Broad_nucleoside_analogue_resistance_implications_for_human_immunodeficiency_virus_type_1_reverse_transcriptase_mutations_at_codons_44_and_118","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/12630105/Broad_nucleoside_analogue_resistance_implications_for_human_immunodeficiency_virus_type_1_reverse_transcriptase_mutations_at_codons_44_and_118"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="4" data-entity-id="20725893" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/20725893/Amino_Acid_Mutation_N348I_in_the_Connection_Subdomain_of_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Confers_Multiclass_Resistance_to_Nucleoside_and_Nonnucleoside_Reverse_Transcriptase_Inhibitors">Amino Acid Mutation N348I in the Connection Subdomain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Confers Multiclass Resistance to Nucleoside and Nonnucleoside Reverse Transcriptase Inhibitors</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="41435815" href="https://independent.academia.edu/ShinichiOka">Shinichi Oka</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Virology, 2008</p><p class="ds-related-work--abstract ds2-5-body-sm">and/or ddI-containing therapy (12.5%; n ‫؍‬ 48; P < 0.0001) and was accompanied with thymidine analogueassociated mutations, e.g., T215Y (n ‫؍‬ 5/6) and the lamivudine resistance mutation M184V (n ‫؍‬ 1/6) in a Japanese cohort. Molecular modeling analysis shows that residue 348 is proximal to the NNRTI-binding pocket and to a flexible hinge region at the base of the p66 thumb that may be affected by the N348I mutation. Our results further highlight the role of connection subdomain residues in drug resistance.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Amino Acid Mutation N348I in the Connection Subdomain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Confers Multiclass Resistance to Nucleoside and Nonnucleoside Reverse Transcriptase Inhibitors","attachmentId":41527654,"attachmentType":"pdf","work_url":"https://www.academia.edu/20725893/Amino_Acid_Mutation_N348I_in_the_Connection_Subdomain_of_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Confers_Multiclass_Resistance_to_Nucleoside_and_Nonnucleoside_Reverse_Transcriptase_Inhibitors","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/20725893/Amino_Acid_Mutation_N348I_in_the_Connection_Subdomain_of_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Confers_Multiclass_Resistance_to_Nucleoside_and_Nonnucleoside_Reverse_Transcriptase_Inhibitors"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="5" data-entity-id="19871232" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/19871232/Amino_acid_mutation_N348I_in_the_connection_subdomain_of_human_immunodeficiency_virus_type_1_reverse_transcriptase_confers_multiclass_resistance_to_nucleoside_">Amino acid mutation N348I in the connection subdomain of human immunodeficiency virus type 1 reverse transcriptase confers multiclass resistance to nucleoside …</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="40681587" href="https://independent.academia.edu/StefanSarafianos">Stefan Sarafianos</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of …, 2008</p><p class="ds-related-work--abstract ds2-5-body-sm">and/or ddI-containing therapy (12.5%; n ‫؍‬ 48; P < 0.0001) and was accompanied with thymidine analogueassociated mutations, e.g., T215Y (n ‫؍‬ 5/6) and the lamivudine resistance mutation M184V (n ‫؍‬ 1/6) in a Japanese cohort. Molecular modeling analysis shows that residue 348 is proximal to the NNRTI-binding pocket and to a flexible hinge region at the base of the p66 thumb that may be affected by the N348I mutation. Our results further highlight the role of connection subdomain residues in drug resistance.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Amino acid mutation N348I in the connection subdomain of human immunodeficiency virus type 1 reverse transcriptase confers multiclass resistance to nucleoside …","attachmentId":40890370,"attachmentType":"pdf","work_url":"https://www.academia.edu/19871232/Amino_acid_mutation_N348I_in_the_connection_subdomain_of_human_immunodeficiency_virus_type_1_reverse_transcriptase_confers_multiclass_resistance_to_nucleoside_","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/19871232/Amino_acid_mutation_N348I_in_the_connection_subdomain_of_human_immunodeficiency_virus_type_1_reverse_transcriptase_confers_multiclass_resistance_to_nucleoside_"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="6" data-entity-id="22069257" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/22069257/The_Human_Immunodeficiency_Virus_Type_1_Nonnucleoside_Reverse_Transcriptase_Inhibitor_Resistance_Mutation_I132M_Confers_Hypersensitivity_to_Nucleoside_Analogs">The Human Immunodeficiency Virus Type 1 Nonnucleoside Reverse Transcriptase Inhibitor Resistance Mutation I132M Confers Hypersensitivity to Nucleoside Analogs</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="43354484" href="https://independent.academia.edu/DwightNissley">Dwight Nissley</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Virology, 2009</p><p class="ds-related-work--abstract ds2-5-body-sm">We previously identified a rare mutation in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT), I132M, which confers high-level resistance to the nonnucleoside RT inhibitors (NNRTIs) nevirapine and delavirdine. In this study, we have further characterized the role of this mutation in viral replication capacity and in resistance to other RT inhibitors. Surprisingly, our data show that I132M confers marked hypersusceptibility to the nucleoside analogs lamivudine (3TC) and tenofovir at both the virus and enzyme levels. Subunit-selective mutagenesis studies revealed that the mutation in the p51 subunit of RT was responsible for the increased sensitivity to the drugs, and transient kinetic analyses showed that this hypersusceptibility was due to I132M decreasing the enzyme's affinity for the natural dCTP substrate but increasing its affinity for 3TC-triphosphate. Furthermore, the replication capacity of HIV-1 containing I132M is severely impaired. This decrease in viral replication capacity could be partially or completely compensated for by the A62V or L214I mutation, respectively. Taken together, these results help to explain the infrequent selection of I132M in patients for whom NNRTI regimens are failing and furthermore demonstrate that a single mutation outside of the polymerase active site and inside of the p51 subunit of RT can significantly influence nucleotide selectivity.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"The Human Immunodeficiency Virus Type 1 Nonnucleoside Reverse Transcriptase Inhibitor Resistance Mutation I132M Confers Hypersensitivity to Nucleoside Analogs","attachmentId":42744605,"attachmentType":"pdf","work_url":"https://www.academia.edu/22069257/The_Human_Immunodeficiency_Virus_Type_1_Nonnucleoside_Reverse_Transcriptase_Inhibitor_Resistance_Mutation_I132M_Confers_Hypersensitivity_to_Nucleoside_Analogs","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/22069257/The_Human_Immunodeficiency_Virus_Type_1_Nonnucleoside_Reverse_Transcriptase_Inhibitor_Resistance_Mutation_I132M_Confers_Hypersensitivity_to_Nucleoside_Analogs"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="7" data-entity-id="27988045" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/27988045/The_K101P_and_K103R_V179D_Mutations_in_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Confer_Resistance_to_Nonnucleoside_Reverse_Transcriptase_Inhibitors">The K101P and K103R/V179D Mutations in Human Immunodeficiency Virus Type 1 Reverse Transcriptase Confer Resistance to Nonnucleoside Reverse Transcriptase Inhibitors</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="52475381" href="https://independent.academia.edu/GuptaSoumi">Soumi Gupta</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Antimicrobial Agents and Chemotherapy, 2006</p><p class="ds-related-work--abstract ds2-5-body-sm">Genotypic patterns associated with nonnucleoside reverse transcriptase inhibitor (NNRTI) resistance in the absence of well-characterized resistance mutations were identified using a database (n > 47,000) of phenotypegenotype data. Among samples with no known NNRTI mutations, the most resistant samples contained K101P (n ‫؍‬ 35) or a combination of K103R and V179D (n ‫؍‬ 41). Site-directed mutagenesis confirmed the importance of these mutations.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"The K101P and K103R/V179D Mutations in Human Immunodeficiency Virus Type 1 Reverse Transcriptase Confer Resistance to Nonnucleoside Reverse Transcriptase Inhibitors","attachmentId":48291365,"attachmentType":"pdf","work_url":"https://www.academia.edu/27988045/The_K101P_and_K103R_V179D_Mutations_in_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Confer_Resistance_to_Nonnucleoside_Reverse_Transcriptase_Inhibitors","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/27988045/The_K101P_and_K103R_V179D_Mutations_in_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Confer_Resistance_to_Nonnucleoside_Reverse_Transcriptase_Inhibitors"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="8" data-entity-id="9542523" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/9542523/Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Mutation_Selection_during_In_Vitro_Exposure_to_Tenofovir_Alone_or_Combined_with_Abacavir_or_Lamivudine">Human Immunodeficiency Virus Type 1 Reverse Transcriptase Mutation Selection during In Vitro Exposure to Tenofovir Alone or Combined with Abacavir or Lamivudine</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="22439662" href="https://missouri.academia.edu/ChrisStone">Chris Stone</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Antimicrobial Agents and Chemotherapy, 2004</p><p class="ds-related-work--abstract ds2-5-body-sm">Mutations selected or deselected during passage of human immunodeficiency virus strain HXB2 or resistant variants with tenofovir (TFV), abacavir (ABC), and lamivudine (3TC) differed depending on the drug combination and virus genotype. In the wild-type virus, TFV-ABC and TFV-3TC selected K65R (with reduced susceptibility to all three inhibitors) and then Y115F. TFV-containing regimens might increase K65R selection, which confers multiple nucleoside reverse transcriptase inhibitor resistance.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Human Immunodeficiency Virus Type 1 Reverse Transcriptase Mutation Selection during In Vitro Exposure to Tenofovir Alone or Combined with Abacavir or Lamivudine","attachmentId":35763405,"attachmentType":"pdf","work_url":"https://www.academia.edu/9542523/Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Mutation_Selection_during_In_Vitro_Exposure_to_Tenofovir_Alone_or_Combined_with_Abacavir_or_Lamivudine","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/9542523/Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Mutation_Selection_during_In_Vitro_Exposure_to_Tenofovir_Alone_or_Combined_with_Abacavir_or_Lamivudine"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div><div class="ds-related-work--container js-wsj-grid-card" data-collection-position="9" data-entity-id="21926028" data-sort-order="default"><a class="ds-related-work--title js-wsj-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/21926028/Genotypic_Phenotypic_and_Modeling_Studies_of_a_Deletion_in_the_beta_3_beta_4_Region_of_the_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Gene_That_Is_Associated_with_Resistance_to_Nucleoside_Reverse_Transcriptase_Inhibitors">Genotypic, Phenotypic, and Modeling Studies of a Deletion in the beta 3-beta 4 Region of the Human Immunodeficiency Virus Type 1 Reverse Transcriptase Gene That Is Associated with Resistance to Nucleoside Reverse Transcriptase Inhibitors</a><div class="ds-related-work--metadata"><a class="js-wsj-grid-card-author ds2-5-body-sm ds2-5-body-link" data-author-id="43166641" href="https://independent.academia.edu/YvetteGirard">Yvette Girard</a></div><p class="ds-related-work--metadata ds2-5-body-xs">Journal of Virology, 2000</p><p class="ds-related-work--abstract ds2-5-body-sm">Point mutations and inserts in the ␤3-␤4 region of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) are associated with resistance to nucleoside analog inhibitors. This report describes HIV-1 strains from seven patients that were found to have a 3-bp deletion in the ␤3-␤4 region of the RT gene. These patient strains also had a mean of 6.2 drug resistance-associated mutations in their RT genes (range, 3 to 10 mutations). The deletion was most frequently found in strains with the Q151M mutation. Nonnucleoside RT inhibitor mutations were found in six of seven strains. Culture-based drug sensitivity assays showed that deletion-containing isolates had reduced susceptibility to four to eight RT inhibitors. Site-directed mutagenesis experiments showed that the deletion alone conferred reduced susceptibility to nucleoside analogs. Changes in the threedimensional models of the RT deletion mutants were consistently observed at the ␤3-␤4 loop and at helices C and E in both the presence and the absence of dTTP. Loss of hydrogen bonds between the RT and dTTP were also observed in the RT deletion mutant. These results suggest that the deletion in the RT gene contributes to resistance to several nucleoside analogs through a complex interaction with other mutations in the RT gene.</p><div class="ds-related-work--ctas"><button class="ds2-5-text-link ds2-5-text-link--inline js-swp-download-button" data-signup-modal="{"location":"wsj-grid-card-download-pdf-modal","work_title":"Genotypic, Phenotypic, and Modeling Studies of a Deletion in the beta 3-beta 4 Region of the Human Immunodeficiency Virus Type 1 Reverse Transcriptase Gene That Is Associated with Resistance to Nucleoside Reverse Transcriptase Inhibitors","attachmentId":42653443,"attachmentType":"pdf","work_url":"https://www.academia.edu/21926028/Genotypic_Phenotypic_and_Modeling_Studies_of_a_Deletion_in_the_beta_3_beta_4_Region_of_the_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Gene_That_Is_Associated_with_Resistance_to_Nucleoside_Reverse_Transcriptase_Inhibitors","alternativeTracking":true}"><span class="material-symbols-outlined" style="font-size: 18px" translate="no">download</span><span class="ds2-5-text-link__content">Download free PDF</span></button><a class="ds2-5-text-link ds2-5-text-link--inline js-wsj-grid-card-view-pdf" href="https://www.academia.edu/21926028/Genotypic_Phenotypic_and_Modeling_Studies_of_a_Deletion_in_the_beta_3_beta_4_Region_of_the_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Gene_That_Is_Associated_with_Resistance_to_Nucleoside_Reverse_Transcriptase_Inhibitors"><span class="ds2-5-text-link__content">View PDF</span><span class="material-symbols-outlined" style="font-size: 18px" translate="no">chevron_right</span></a></div></div></div></div><div class="ds-sticky-ctas--wrapper js-loswp-sticky-ctas hidden"><div class="ds-sticky-ctas--grid-container"><div class="ds-sticky-ctas--container"><button class="ds2-5-button js-swp-download-button" data-signup-modal="{"location":"continue-reading-button--sticky-ctas","attachmentId":49012142,"attachmentType":"pdf","workUrl":null}">See full PDF</button><button class="ds2-5-button ds2-5-button--secondary js-swp-download-button" data-signup-modal="{"location":"download-pdf-button--sticky-ctas","attachmentId":49012142,"attachmentType":"pdf","workUrl":null}"><span class="material-symbols-outlined" style="font-size: 20px" translate="no">download</span>Download PDF</button></div></div></div><div class="ds-below-fold--grid-container"><div class="ds-work--container js-loswp-embedded-document"><div class="attachment_preview" data-attachment="Attachment_49012142" style="display: none"><div class="js-scribd-document-container"><div class="scribd--document-loading js-scribd-document-loader" style="display: block;"><img alt="Loading..." src="//a.academia-assets.com/images/loaders/paper-load.gif" /><p>Loading Preview</p></div></div><div style="text-align: center;"><div class="scribd--no-preview-alert js-preview-unavailable"><p>Sorry, preview is currently unavailable. You can download the paper by clicking the button above.</p></div></div></div></div><div class="ds-sidebar--container js-work-sidebar"><div class="ds-related-content--container"><h2 class="ds-related-content--heading">Related papers</h2><div class="ds-related-work--container js-related-work-sidebar-card" data-collection-position="0" data-entity-id="13481924" data-sort-order="default"><a class="ds-related-work--title js-related-work-grid-card-title ds2-5-body-md ds2-5-body-link" href="https://www.academia.edu/13481924/Characterization_and_Structural_Analysis_of_Novel_Mutations_in_Human_Immunodeficiency_Virus_Type_1_Reverse_Transcriptase_Involved_in_the_Regulation_of_Resistance_to_Nonnucleoside_Inhibitors">Characterization and Structural Analysis of Novel Mutations in Human Immunodeficiency Virus Type 1 Reverse Transcriptase Involved in the Regulation of Resistance to Nonnucleoside Inhibitors</a><div class="ds-related-work--metadata"><a class="js-related-work-grid-card-author 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