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CD4 receptor diversity represents an ancient protection mechanism against primate lentiviruses.

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Title: CD4 receptor diversity represents an ancient protection mechanism against primate lentiviruses.
Authors: Russell, Ronnie M.1,2, Bibollet-Ruche, Frederic1, Liu, Weimin1, Sherrill-Mix, Scott1,2, Yingying Li, Connell, Jesse1, Loy, Dorothy E.1,2, Trimboli, Stephanie1,2, Smith, Andrew G.1, Avitto, Alexa N.1, Gondim, Marcos V. P.1, Plenderleith, Lindsey J.3,4, Wetzel, Katherine S.2, Collman, Ronald G.1,2, Ayouba, Ahidjo5, Esteban, Amandine5, Peeters, Martine5, Kohler, William J.6, Miller, Richard A.6, François-Souquiere, Sandrine7
Source: Proceedings of the National Academy of Sciences of the United States of America. 3/30/2021, Vol. 118 Issue 13, p1-12. 12p.
Subjects: CD4 antigen, HIV infections, Lentiviruses, Primates, Value (Economics), Commercial products, Viral envelopes
Abstract: Infection with human and simian immunodeficiency viruses (HIV/SIV) requires binding of the viral envelope glycoprotein (Env) to the host protein CD4 on the surface of immune cells. Although invariant in humans, the Env binding domain of the chimpanzee CD4 is highly polymorphic, with nine coding variants circulating in wild populations. Here, we show that within-species CD4 diversity is not unique to chimpanzees but found in many African primate species. Characterizing the outermost (D1) domain of the CD4 protein in over 500 monkeys and apes, we found polymorphic residues in 24 of 29 primate species, with as many as 11 different coding variants identified within a single species. D1 domain amino acid replacements affected SIV Env-mediated cell entry in a single-round infection assay, restricting infection in a strain- and allele-specific fashion. Several identical CD4 polymorphisms, including the addition of N-linked glycosylation sites, were found in primate species from different genera, providing striking examples of parallel evolution. Moreover, seven different guenons (Cercopithecus spp.) shared multiple distinct D1 domain variants, pointing to long-term trans-specific polymorphism. These data indicate that the HIV/SIV Env binding region of the primate CD4 protein is highly variable, both within and between species, and suggest that this diversity has been maintained by balancing selection for millions of years, at least in part to confer protection against primate lentiviruses. Although long-term SIV-infected species have evolved specific mechanisms to avoid disease progression, primate lentiviruses are intrinsically pathogenic and have left their mark on the host genome. [ABSTRACT FROM AUTHOR]
Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: CD4 receptor diversity represents an ancient protection mechanism against primate lentiviruses.
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  Data: <searchLink fieldCode="DE" term="%22CD4+antigen%22">CD4 antigen</searchLink><br /><searchLink fieldCode="DE" term="%22HIV+infections%22">HIV infections</searchLink><br /><searchLink fieldCode="DE" term="%22Lentiviruses%22">Lentiviruses</searchLink><br /><searchLink fieldCode="DE" term="%22Primates%22">Primates</searchLink><br /><searchLink fieldCode="DE" term="%22Value+%28Economics%29%22">Value (Economics)</searchLink><br /><searchLink fieldCode="DE" term="%22Commercial+products%22">Commercial products</searchLink><br /><searchLink fieldCode="DE" term="%22Viral+envelopes%22">Viral envelopes</searchLink>
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  Data: Infection with human and simian immunodeficiency viruses (HIV/SIV) requires binding of the viral envelope glycoprotein (Env) to the host protein CD4 on the surface of immune cells. Although invariant in humans, the Env binding domain of the chimpanzee CD4 is highly polymorphic, with nine coding variants circulating in wild populations. Here, we show that within-species CD4 diversity is not unique to chimpanzees but found in many African primate species. Characterizing the outermost (D1) domain of the CD4 protein in over 500 monkeys and apes, we found polymorphic residues in 24 of 29 primate species, with as many as 11 different coding variants identified within a single species. D1 domain amino acid replacements affected SIV Env-mediated cell entry in a single-round infection assay, restricting infection in a strain- and allele-specific fashion. Several identical CD4 polymorphisms, including the addition of N-linked glycosylation sites, were found in primate species from different genera, providing striking examples of parallel evolution. Moreover, seven different guenons (Cercopithecus spp.) shared multiple distinct D1 domain variants, pointing to long-term trans-specific polymorphism. These data indicate that the HIV/SIV Env binding region of the primate CD4 protein is highly variable, both within and between species, and suggest that this diversity has been maintained by balancing selection for millions of years, at least in part to confer protection against primate lentiviruses. Although long-term SIV-infected species have evolved specific mechanisms to avoid disease progression, primate lentiviruses are intrinsically pathogenic and have left their mark on the host genome. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Proceedings of the National Academy of Sciences of the United States of America is the property of National Academy of Sciences and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1073/pnas.2025914118
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      – Code: eng
        Text: English
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        PageCount: 12
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      – SubjectFull: CD4 antigen
        Type: general
      – SubjectFull: HIV infections
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      – SubjectFull: Lentiviruses
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      – SubjectFull: Primates
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      – SubjectFull: Value (Economics)
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      – SubjectFull: Commercial products
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      – SubjectFull: Viral envelopes
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      – TitleFull: CD4 receptor diversity represents an ancient protection mechanism against primate lentiviruses.
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