Role of the HIV gp120 conserved domain 5 in processing and viral entry

Biochemistry

Volumn 47, Issue 30, 2008, Pages 7788-7795

  Sen, Jayita ^a   Jacobs, Amy ^b   Caffrey, Michael ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; DRUG DELIVERY; DRUG DOSAGE;

ALANINE SCANNING MUTAGENESIS; AMERICAN CHEMICAL SOCIETY (ACS); DELETERIOUS EFFECTS; DRUG DISCOVERIES; ENVELOPE FUNCTIONS; GAIN-OF FUNCTION; MEMBRANE FUSION; MUTATIONAL EFFECTS; WILD-TYPE (WT);

CHEMOTHERAPY;

ALANINE; ENVELOPE PROTEIN; GLYCOPROTEIN GP 120; MUTANT PROTEIN;

ARTICLE; CONTROLLED STUDY; EMBRYO; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS; MEMBRANE FUSION; MUTAGENESIS; MUTAGENIC ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STRUCTURE; VIRUS ENTRY; VIRUS ENVELOPE; VIRUS MUTATION; WILD TYPE;

AMINO ACID SEQUENCE; ANTIGENS, CD4; BLOTTING, WESTERN; CELL LINE; CONSERVED SEQUENCE; GLYCOSYLATION; HIV; HIV ENVELOPE PROTEIN GP120; HUMANS; LINEAR MODELS; LUCIFERASES; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 48249130042     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800227z     Document Type: Article

References (31)

1. Gallo, S., Finnegan, C., Viard, M., Raviv, Y., Dimitrov, A., Rawat, S., Puri, A., Durrell, S., and Blumenthal, R. (2003) The HIV Env-mediated fusion reaction. Biochim. Biophys. Acta 1614, 36-50.
2. Freed, E., and Martin, M. (1995) The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection. J. Biol. Chem. 270, 23833-23836.
3. Bazan, H., Alkhatib, G., Broder, C., and Berger, E. (1998) Patterns of CCR5, CXCR4, and CCR3 usage by envelope glycoproteins from human immunodeficiency virus type-1 primary isolates. J. Virol. 72, 4485-4491.
4. Björndal, A., Deng, H., Jansson, M., Fiore, J. R., Colognesi, C., Karlsson, A., Albert, J., Scarlatti, G., Littman, D. R., and Fenyo, E. M. (1997) Coreceptor usage of primary human immunodeficiency virus type 1 isolates varies according to biological phenotype. J. Virol. 71, 7478-7487.
5. Chan, D., Fass, D., Berger, J., and Kim, P. (1997) Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273.
6. Weissenhorn, W., Dessen, A., Harrison, S., Skehel, J., and Wiley, D. (1997) Atomic structure of the ectodomain from HIV-1 gp41. Nature 387, 426-430.
7. Tan, K., Liu, J.-H., Wang, J.-H., Shen, S., and Lu, M. (1997) Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. U.S.A. 94, 12203-12308.
8. Caffrey, M., Cai, M., Kaufman, J., Stahl, S., Wingfield, P., Gronenborn, A., and Clore, G. (1997) Determination of the secondary structure and global topology of the 44 kDa ectodomain of gp41 of the simian immunodeficiency virus by multidimensional nuclear magnetic resonance spectroscopy. J. Mol. Biol. 271, 819-826.
9. Caffrey, M., Cai, M., Kaufman, J., Stahl, S., Wingfield, P., Covell, D., Gronenborn, A., and Clore, G. (1998) Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J. 17, 4572-4584.
10. Malashkevich, V., Chan, D., Chutkowski, C., and Kim, P. (1998) Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc. Natl. Acad. Sci. U.S.A. 95, 9134-9139.
11. Yang, Z., Mueser, T., Kaufman, J., Stahl, S., Wingfield, P., and Hyde, C. (1999) The crystal structure of the SIV gp41 ectodomain at 1.47 Å resolution. Struct. Biol. 126, 131-144.
12. Caffrey, M. (2001) Model for the structure of the HIV gp41 ectodomain: insight into the intermolecular interactions of the gp41 loop. Biochim. Biophys. Acta 1536, 116-122.
13. Kwong, P., Wyatt, R., Robinson, T., Sweet, R., Sodroski, J., and Hendrickson, W. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393, 648-659.
14. Huang, C., Tang, M., Zhang, M., Majeed, S., Montabana, E., Stanfield, R., Dimitrov, D., Korber, B., Sodroski, J., and Wilson, I. (2005) Structure of a V3-containing HIV-1 gp120 core. Science 310, 1025-1028.
15. Chen, B., Vogan, E., Gong, H., Skehel, J., Wiley, D., and Harrison, S. (2005) Structure of an unliganded simian immunodeficiency virus gp120 core. Nature 433, 834-841.
16. 2-terminal 31 amino acids of human immunodeficiency virus type-1 envelope protein gp120 contain a potential gp41 contact site. J. Virol. 65, 2682-2685.
17. Helseth, E., Olshevsky, U., Furman, C., and Sodroski, J. (1991) Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp4 L transmembrane glycoprotein. J. Virol. 65, 2119-2123.
18. Binley, J., Sanders, R., Clas, B., Schuelke, N., Master, A., Guo, Y., Kajumo, F., Anselma, J., Maddon, P., Olson, W., and Moore, J. (2000) A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J. Virol. 74, 627-643.
19. Guilhaudis, L., Jacobs, A., and Caffrey, M. (2002) Solution structure of the HIV gp120 C5 domain. Eur. J. Biochem. 269, 4860-4867.
20. Page, K., Landau, N., and Littman, D. (1990) Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity. J. Virol. 64, 5270-5276.
21. Connor, R., Chen, B., Choe, S., and Landau, N. (1995) Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206, 935-944.
22. Abacioglu, Y. H., Fouts, T. R., Laman, J. D., Claassen, E., Pincus, S. H., Moore, J. P., Roby, C. A., Kamin-Lewis, R., and Lewis, G. K. (1994) Epitope mapping and topology of baculovirus-expressed HIV-1 gp160 determined with a panel of murine monoclonal antibodies. AIDS Res. Hum. Retroviruses 10, 371-381.
23. Douglas, N., Munro, G., and Daniels, R. (1997) HIV/SIV glycoproteins: structure-function relationships. J. Mol. Biol. 273, 122-149.
24. McCune, J. M., Rabin, L. B., Feinberg, M. B., Lieberman, M., Kosek, J. C., Reyes, G. R., and Weissman, I. L. (1988) Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell 53, 55-67.
25. Freed, E. O., Myers, D. J., and Risser, R. (1989) Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160. J. Virol. 63, 4670-4675.
26. Bosch, V., and Pawlita, M. (1990) Mutational analysis of the human immunodeficiency virus type 1 env gene product proteolytic cleavage site. J. Virol. 64, 2337-2344.
27. Jacobs, A., Sen, J., Rong, L., and Caffrey, M. (2005) Alanine scanning mutagenesis of the HIV gp41 loop. J. Biol. Chem. 280, 27284-27288.
28. Sen, J., Jacobs, A., Jiang, H., Rong, L., and Caffrey, M. (2007) The disulfide bond is critical to the furin recognition site of HIV gp160. Protein Sci. 16, 1236-1241.
29. Schenten, D., Marcon, L., Karlsson, G., Parolin, C., Kodama, T., Gerard, N., and Sodroski, J. (1999) Effects of soluble CD4 on simian immunodeficiency virus infection of CD4-positive and CD4-negative cells. J. Virol. 73, 5373-5380.
30. Abrahamyan, L., Markosyan, R., Moore, J., Cohen, F., and Melikyan, G. (2003) Human immunodeficiency virus type 1 Env with an intersubunit disulfide bond engages coreceptors but requires bond reduction after engagement to induce fusion. J. Virol. 77, 5829-5836.
31. Binley, J., Cayanan, C., Wiley, C., Schulke, N., Olson, W., and Burton, D. (2003) Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J. Virol. 77, 5678-5684.