Amino- and Carboxyl-Terminal CCR5 Mutations in Brazilian HIV-1-Infected Women and Homology Model of p.L55Q CCR5 Mutant.

dc.creatorCosta, Giselle Calasans de Souza
dc.creatorNunes, Marcio Roberto Teixeira
dc.creatorJesus, Jaqueline Goes
dc.creatorNovaes, Thiago
dc.creatorCardoso, Jedson Ferreira
dc.creatorSousa Júnior, Edivaldo Costa
dc.creatorSantos, Edson de Souza
dc.creatorCastro Filho, Bernardo Galvão
dc.creatorZanette, Dalila Lucíola
dc.creatorGonçalves, Marilda de Souza
dc.creatorAlcantara, Luiz Carlos Júnior
dc.date2016-03-23T12:55:09Z
dc.date2016-03-23T12:55:09Z
dc.date2015
dc.date.accessioned2023-09-26T20:53:14Z
dc.date.available2023-09-26T20:53:14Z
dc.identifierCOSTA, G. C. S. et al. Amino- and Carboxyl-Terminal CCR5 Mutations in Brazilian HIV-1-Infected Women and Homology Model of p.L55Q CCR5 Mutant. AIDS Research Human Retroviruses, v. 31, n. 7, p. 685-691, 2015.
dc.identifier1931-8405
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/13252
dc.identifier10.1089/aid.2014.0140
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8865618
dc.descriptionGenetic factors from an HIV-1 host can affect the rate of progression to AIDS and HIV infection. To investigate the frequency of mutations in the CCR5 gene, HIV-1 samples from infected women and uninfected individuals were selected for sequencing of the CCR5 gene regions encoding the N- and C-terminal protein domains. Physicochemical CCR5 modeling and potential protein domain analysis were performed in order to evaluate the impact of the mutations found in the properties and structure of CCR5. The p.L55Q mutation in the N-terminal protein domain was observed only in uninfected individuals, with an allelic frequency of 1.8%. Physicochemical analysis revealed that the p.L55Q mutation magnified the flexibility and accessibility profiles and the modeling of CCR5 structures showed resulting in a small deviation to the right, as well as a hydrophobic to hydrophilic property alteration. The p.L55Q mutation also resulted in a slight modification of the electrostatic load of this region. Additionally, three novel silent mutations were found at the C-terminal coding region among HIV-1-infected women. The results suggest that the p.L55Q mutation might alter CCR5 conformation. Further studies should be conducted to verify the role of this mutation in HIV-1 susceptibility.
dc.formatapplication/pdf
dc.languageeng
dc.publisherMary Ann Liebert
dc.rightsopen access
dc.subjectMutação
dc.subjectGenética
dc.subjectHIV-1
dc.subjectInfecção
dc.subjectFeminino
dc.subjectReceptores CCR5
dc.titleAmino- and Carboxyl-Terminal CCR5 Mutations in Brazilian HIV-1-Infected Women and Homology Model of p.L55Q CCR5 Mutant.
dc.typeArticle


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