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      The crystal structure of HIV CRF07 B'/C gp41 reveals a hyper-mutant site in the middle of HR2 heptad repeat.

      Biology

      Amino Acids, genetics, Cell Fusion, China, Crystallography, X-Ray, DNA Mutational Analysis, HIV Envelope Protein gp41, chemistry, metabolism, HIV-1, isolation & purification, physiology, Humans, Models, Molecular, Mutation, Protein Conformation, Sequence Alignment, Virus Internalization

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          Abstract

          HIV CRF07 B'/C is a strain circulating mainly in northwest region of China. The gp41 region of CRF07 is derived from a clade C virus. In order to compare the difference of CRF07 gp41 with that of typical clade B virus, we solved the crystal structure of the core region of CRF07 gp41. Compared with clade B gp41, CRF07 gp41 evolved more basic and hydrophilic residues on its helix bundle surface. Based on sequence alignment, a hyper-mutant cluster located in the middle of HR2 heptads repeat was identified. The mutational study of these residues revealed that this site is important in HIV mediated cell-cell fusion and plays critical roles in conformational changes during viral invasion. © 2013 Elsevier Inc. All rights reserved.

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          Journal
          24074570
          10.1016/j.virol.2013.07.024

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