Soluble gC1q-R/p33, a cell protein that binds to the globular "Heads" of C1q, effectively inhibits the growth of HIV-1 strains in cell cultures

Clinical Immunology and Immunopathology

Volumn 99, Issue 2, 2001, Pages 222-231

  Szabo J ^a   Cervenak L ^b   Toth F D ^a   Prohaszka Z ^b,c   Horvath L ^b   Kerekes, K ^d   Beck, Z ^a   Bacsi A ^a   Erdei, A ^d   Peerschke, E I B ^e   Fust G ^b,c   Ghebrehiwet, B ^f  

^a UNIVERSITY OF DEBRECEN   (Hungary)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^c SEMMELWEIS UNIVERSITY OF MEDICINE   (Hungary)

^d EÖTVÖS LORÁND UNIVERSITY   (Hungary)

^e WEILL CORNELL MEDICAL COLLEGE   (United States)

^f STONY BROOK UNIVERSITY   (United States)

Author keywords

CD4; GClq receptor; HIV 1; Inhibition; Viral entry

Indexed keywords

ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; C1QBP PROTEIN, HUMAN; CARRIER PROTEIN; CD4 ANTIGEN; COMPLEMENT 1Q RECEPTOR; COMPLEMENT COMPONENT C1Q; COMPLEMENT RECEPTOR; GLYCOPROTEIN GP 120; HERMES ANTIGEN; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; BINDING SITE; CELL LINE; CHEMISTRY; DRUG EFFECT; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IMMUNOLOGY; MACROPHAGE; METABOLISM; PATHOGENICITY; PHYSIOLOGY; SOLUBILITY; T LYMPHOCYTE; VIROLOGY; VIRUS REPLICATION;

ANTI-HIV AGENTS; ANTIGENS, CD4; ANTIGENS, CD44; BINDING SITES; CARRIER PROTEINS; CELL LINE; COMPLEMENT C1Q; HIV ENVELOPE PROTEIN GP120; HIV INFECTIONS; HIV-1; HUMANS; MACROPHAGES; MEMBRANE GLYCOPROTEINS; MITOCHONDRIAL PROTEINS; RECEPTORS, COMPLEMENT; RECOMBINANT PROTEINS; SOLUBILITY; T-LYMPHOCYTES; VIRUS REPLICATION;

EID: 16344362662     PISSN: 00901229     EISSN: None     Source Type: Journal    
DOI: 10.1006/clim.2001.5013     Document Type: Article

References (15)

1. Ebenbichler, C. F., Thielens, E. M., Vornhagen, R., Marschang, P., Arlaud, G. J., and Dierich, M. P., Human immunodeficiency virus type 1 activates the classical pathway of complement by direct Cl binding through specific sites in the transmembrane glycoprotein gp41. J. Exp. Med. 174, 1417-1424, 1991.
2. Hidvégi, T., Prohászka, Z., Ujhelyi, E., Thielens, N. M., Dierich, M. P., Hampl, H., Arlaud, G. J., Nagy, K, and Füst, G., Studies on the mechanism of complement-mediated inhibition of anti body binding to HIV gp41. Clin. Exp. Immunol. 94, 490-493, 1993.
3. Thielens, N. M., Bally, L M., Ebenbichler, C. F., Dierich, M. P., and Arlaud, G. J., Further characterization of the interaction between the Clq subcomponent of human Cl and the transmembrane envelope glycoprotein gp41 of HIV-1. J. Immunol. 151, 6583-6592, 1993.
4. Stoiber, H., Thielens, N., Ebenbichler, C. F., Arlaud, G. J., and Dierich, M. P., The envelope glycoprotein of HIV-1 gp120 and human complement protein Clq bind to the same peptides derived from three different regions of gp41, the transmembrane glycoprotein of HIV-1, and share antigenic homology. Eur. J. Immunol. 24, 294-300, 1994.
5. Prohászka, Z., Nemes, J., Hidvégi, T., Tóth, F. D., Kerekes, K, Erdei, A., Szabó, J., Ujhelyi, E., Thielens, N., Dierich, M. P., Spath, P., Ghebrehiwet, B., Hampl, H., Kiss, J., Arlaud, G. J., and Füst, G., Two parallel routes of the complement-mediated antibody-dependent enhancement of HIV-1 infection. AIDS 11, 949-958, 1997.
6. Metlas, R., Skerk., V., Velikovic, V., Colombatti, A., and Pongor, S., Immunoglobulin-like domain of HIV-1 envelope glycoprotein gp120 encodes putative internal image of some common human proteins. Viral Immunol. 7, 215-219, 1994.
7. Ghebrehiwet, B., Lim, B.-L., Peerschke, E. I. B., Willis, A. C., and Reid, K. B. M., Isolation, cDNA cloning, and overexpression of a 33-kDa cell surface glycoprotein that binds to the globular "heads" of Clq. J. Exp. Med. 179, 1809-1821, 1994.
8. Luo, Y., Yu, H., and Peterlin, B. M., Cellular protein modulates effects of human immunodeficiency virus type 1 Rev. J. Virol. 68, 3850-3856, 1994.
9. Yu, L., Loewenstein, P. M., Zhang, Z., and Green, G., In vitro interaction of the human immunodeficiency virus type 1 tat transactivator and the general transcription factor TFIIB with the cellular protein TAP. J. Virol. 69, 3017-3023, 1995.
10. Mathews, D. A., and Russel, W. C., Adenovirus core protein V interacts with p32 protein which is associated with both the mitochondria and the nucleus. J. Gen. Virol. 79, 1677-1685, 1998.
11. Wang, Y., Finnan, J. E., Middeldorp, J. M., and Hayward, S. D., p32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus. Virology 236, 18-29, 1997.
12. Bruni, R., and Roizman, B., Open reading frame P-A herpes simplex virus gene repressed during productive infection encodes a protein that binds a splicing factor and reduces synthesis of viral proteins made from spliced mRNA. Proc. Natl. Acad. Sci. USA 93, 10423-10427, 1996.
13. Braun, L., Ghebrehiwet, B., and Cossart, P., gClq-R/p32, a Clqbinding protein is a novel receptor for Listeria monocytogenes. EMBO J. 19, 1458-1466, 2000.
14. Nguyen, T., Ghebrehiwet, B., and Peerschke, E. I. B., Staphylococcus aureus protein A recognizes platelet gClq-R/p33: A novel mechanism for Staphylococcus interactions with platelets. Infect. Immun. 68, 2061-2068, 2000.
15. Berger, E. A., Dors, R. W., Fenyo, E. M., Korber, B. T., Littman, D. L., Moore, J. P., Sattentau, Q. J., Schitmaker, H., Sodroski, J., and Weis, R. A., A new classification of HIV-1. Nature 391, 240-243, 1998.