Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/13252
Title: Amino- and Carboxyl-Terminal CCR5 Mutations in Brazilian HIV-1-Infected Women and Homology Model of p.L55Q CCR5 Mutant.
Authors: Costa, Giselle Calasans de Souza
Nunes, Marcio Roberto Teixeira
Jesus, Jaqueline Goes
Novaes, Thiago
Cardoso, Jedson Ferreira
Sousa Júnior, Edivaldo Costa
Santos, Edson de Souza
Castro Filho, Bernardo Galvão
Zanette, Dalila Lucíola
Gonçalves, Marilda de Souza
Alcantara, Luiz Carlos Júnior
Affilliation: Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil / Universidade Federal da Bahia. Salvador, BA, Brasil
Evandro Chagas Institute. Bioinformatic Core. Center for Technological Innovation. Belém, PA, Brasil
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Evandro Chagas Institute. Bioinformatic Core. Center for Technological Innovation. Belém, PA, Brasil
Evandro Chagas Institute. Bioinformatic Core. Center for Technological Innovation. Belém, PA, Brasil
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil / Universidade Federal da Bahia. Salvador, BA, Brasil
Fundação Oswaldo Cruz. Centro de Pesquisas Gonçalo Moniz. Salvador, BA, Brasil
Abstract: Genetic 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.
keywords: Mutação
Genética
HIV-1
Infecção
Feminino
Receptores CCR5
Issue Date: 2015
Publisher: Mary Ann Liebert
Citation: COSTA, 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.
DOI: 10.1089/aid.2014.0140
ISSN: 1931-8405
Copyright: open access
Appears in Collections:IGM - Artigos de Periódicos

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