Abstract:
:Natural evolution in primate lentiviral reverse transcriptase (RT) appears to have been constrained by the necessity to maintain function within an asymmetric protein composed of two identical primary amino acid sequences (66 kDa), of which one is cleaved (51 kDa). In this study, a detailed phylogenetic analysis now segregates groups O and M into clusters based on a cysteine or tyrosine residue located at position 181 of RT and linked to other signature residues. Divergent evolution of two group O (C181 or Y181) and the main (Y181 only) HIV-1 lineages did not appreciably impact RT activity or function. Group O RT structural models, based on group M subtype B RT crystal structures, revealed that most evolutionarily linked amino acids appear on a surface-exposed region of one subunit while in a noncatalytic RT pocket of the other subunit. This pocket binds nonnucleoside RT inhibitors (NNRTI); therefore, NNRTI sensitivity was used to probe enzyme differences in these group O and M lineages. In contrast to observations showing acquired drug resistance associated with fitness loss, the C181Y mutation in the C181 group O lineage resulted in a loss of intrinsic NNRTI resistance and was accompanied by fitness loss. Other mutations linked to the NNRTI-resistant C181 lineage also resulted in altered NNRTI sensitivity and a net fitness cost. Based on RT asymmetry and conservation of the intricate reverse transcription process, millions of years of divergent primate lentivirus evolution may be constrained to discrete mutations that appear primarily in the nonfunctional, solvent-accessible NNRTI binding pocket.
journal_name
J Viroljournal_title
Journal of virologyauthors
Tebit DM,Lobritz M,Lalonde M,Immonen T,Singh K,Sarafianos S,Herchenröder O,Kräusslich HG,Arts EJdoi
10.1128/JVI.00991-10subject
Has Abstractpub_date
2010-10-01 00:00:00pages
9817-30issue
19eissn
0022-538Xissn
1098-5514pii
JVI.00991-10journal_volume
84pub_type
杂志文章abstract::Hemagglutinin (HA) of H3N2/1968 pandemic influenza viruses differs from the putative avian precursor by seven amino acid substitutions. Substitutions Q226L and G228S are known to be essential for adaptation of avian HA to mammals. We found that introduction of avian-virus-like amino acids at five other HA positions (p...
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journal_title:Journal of virology
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pub_type: 杂志文章
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更新日期:2007-08-01 00:00:00
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journal_title:Journal of virology
pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:2012-01-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1984-08-01 00:00:00
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pub_type: 杂志文章
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更新日期:1974-01-01 00:00:00
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pub_type: 杂志文章
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更新日期:1984-03-01 00:00:00
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journal_title:Journal of virology
pub_type: 杂志文章
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更新日期:2003-09-01 00:00:00
abstract::A variant form of splicing of RNA crossing the Epstein-Barr virus (EBV) BZLF1 gene was observed in the late productive cycle of EBV. This splice omits the middle exon of BZLF1 and joins the outer two exons of BZLF1 in frame, but the shortened form of BZLF1 protein (Z delta) could not be detected in natural EBV infecti...
journal_title:Journal of virology
pub_type: 杂志文章
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pub_type: 杂志文章
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