Abstract
Background:HIV-1 infectivity is decreased by specific mutations that alter the hydrophobicity level in the HIV-1 gp41 loop core. Results:Antibody recognition, disulfide-bond formation, and lipid mixing of loop domain peptides are strongly affected by these mutations. Conclusion:The hydrophobic core maintains proper function and structure of the loop region. Significance:A better understanding of the membrane fusion mechanism of HIV and similar viruses is provided.
Original language | English |
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Pages (from-to) | 29143-29150 |
Number of pages | 8 |
Journal | Journal of Biological Chemistry |
Volume | 288 |
Issue number | 40 |
DOIs | |
State | Published - 4 Oct 2013 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology