Inhibition of HIV-1 infection in vitro by monoclonal antibodies to the complement receptor type 3 (CR3)

An accessory role for CR3 during virus entry?

Heribert Stoiber, Ines Frank, Martin Spruth, Michael Schwendinger, Brigitte Mullauer, Jörg M. Windisch, Rainer Schneider, Hermann Katinger, I. Andó, Manfred P. Dierich

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Adhesion molecules are known to contribute to infectivity of HIV-1. Here we tested whether the complement receptor type 3 (CR3, CD11b), an α(m)β2 integrin, plays an accessory role in the infection process of HIV-1, because ICAM-1, a ligand of CR3, is present on the envelope of HIV-1. In addition, the vital transmembrane protein gp41 shares four regions of homology with the complement component C3, a further CR3 ligand. Infection of PBMCs with HIV- IIIB and primary isolates was partially inhibited by anti-CR3 antibodies. A peptide derived from the complement component C3, covering the CR3-binding site of C3 and sharing strong similarity to the immunosuppressive region of gp41, significantly reduced the HIV-1 titer in infection assays. Recombinant soluble gp41 (rsgp41) and the peptide covering the immunosuppressive domain of gp41 inhibited the rosetting of iC3b-coated sheep erythrocytes with U937 via complement receptors (CRs) with an efficiency comparable to monoclonal anti-CR antibodies. In addition, sub-populations of CD4 + and CD8 + T-cells isolated from HIV-infected individuals were found to upregulate CR3 as determined by FACS analysis and on the mRNA level. Since gp41 has been implicated in viral fusion, an interaction of its C3-homology region in gp41 or an interaction of ICAM on the surface of free virus with CRs might contribute to facilitate viral entry.

Original languageEnglish
Pages (from-to)855-863
Number of pages9
JournalMolecular Immunology
Volume34
Issue number12-13
DOIs
Publication statusPublished - 1997

Fingerprint

Macrophage-1 Antigen
Virus Internalization
HIV Infections
HIV-1
Monoclonal Antibodies
Complement Receptors
Complement C3
Immunosuppressive Agents
Infection
HIV
Complement C3b
Ligands
Peptides
In Vitro Techniques
Antibodies
Intercellular Adhesion Molecule-1
Integrins
Sheep
Up-Regulation
Erythrocytes

Keywords

  • Adhesion molecule
  • CR3
  • gp41
  • HIV

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

Inhibition of HIV-1 infection in vitro by monoclonal antibodies to the complement receptor type 3 (CR3) : An accessory role for CR3 during virus entry? / Stoiber, Heribert; Frank, Ines; Spruth, Martin; Schwendinger, Michael; Mullauer, Brigitte; Windisch, Jörg M.; Schneider, Rainer; Katinger, Hermann; Andó, I.; Dierich, Manfred P.

In: Molecular Immunology, Vol. 34, No. 12-13, 1997, p. 855-863.

Research output: Contribution to journalArticle

Stoiber, H, Frank, I, Spruth, M, Schwendinger, M, Mullauer, B, Windisch, JM, Schneider, R, Katinger, H, Andó, I & Dierich, MP 1997, 'Inhibition of HIV-1 infection in vitro by monoclonal antibodies to the complement receptor type 3 (CR3): An accessory role for CR3 during virus entry?', Molecular Immunology, vol. 34, no. 12-13, pp. 855-863. https://doi.org/10.1016/S0161-5890(97)00108-9
Stoiber, Heribert ; Frank, Ines ; Spruth, Martin ; Schwendinger, Michael ; Mullauer, Brigitte ; Windisch, Jörg M. ; Schneider, Rainer ; Katinger, Hermann ; Andó, I. ; Dierich, Manfred P. / Inhibition of HIV-1 infection in vitro by monoclonal antibodies to the complement receptor type 3 (CR3) : An accessory role for CR3 during virus entry?. In: Molecular Immunology. 1997 ; Vol. 34, No. 12-13. pp. 855-863.
@article{43abcda2fddf4cc4973ac9e6e1a7c7a1,
title = "Inhibition of HIV-1 infection in vitro by monoclonal antibodies to the complement receptor type 3 (CR3): An accessory role for CR3 during virus entry?",
abstract = "Adhesion molecules are known to contribute to infectivity of HIV-1. Here we tested whether the complement receptor type 3 (CR3, CD11b), an α(m)β2 integrin, plays an accessory role in the infection process of HIV-1, because ICAM-1, a ligand of CR3, is present on the envelope of HIV-1. In addition, the vital transmembrane protein gp41 shares four regions of homology with the complement component C3, a further CR3 ligand. Infection of PBMCs with HIV- IIIB and primary isolates was partially inhibited by anti-CR3 antibodies. A peptide derived from the complement component C3, covering the CR3-binding site of C3 and sharing strong similarity to the immunosuppressive region of gp41, significantly reduced the HIV-1 titer in infection assays. Recombinant soluble gp41 (rsgp41) and the peptide covering the immunosuppressive domain of gp41 inhibited the rosetting of iC3b-coated sheep erythrocytes with U937 via complement receptors (CRs) with an efficiency comparable to monoclonal anti-CR antibodies. In addition, sub-populations of CD4 + and CD8 + T-cells isolated from HIV-infected individuals were found to upregulate CR3 as determined by FACS analysis and on the mRNA level. Since gp41 has been implicated in viral fusion, an interaction of its C3-homology region in gp41 or an interaction of ICAM on the surface of free virus with CRs might contribute to facilitate viral entry.",
keywords = "Adhesion molecule, CR3, gp41, HIV",
author = "Heribert Stoiber and Ines Frank and Martin Spruth and Michael Schwendinger and Brigitte Mullauer and Windisch, {J{\"o}rg M.} and Rainer Schneider and Hermann Katinger and I. And{\'o} and Dierich, {Manfred P.}",
year = "1997",
doi = "10.1016/S0161-5890(97)00108-9",
language = "English",
volume = "34",
pages = "855--863",
journal = "Molecular Immunology",
issn = "0161-5890",
publisher = "Elsevier Limited",
number = "12-13",

}

TY - JOUR

T1 - Inhibition of HIV-1 infection in vitro by monoclonal antibodies to the complement receptor type 3 (CR3)

T2 - An accessory role for CR3 during virus entry?

AU - Stoiber, Heribert

AU - Frank, Ines

AU - Spruth, Martin

AU - Schwendinger, Michael

AU - Mullauer, Brigitte

AU - Windisch, Jörg M.

AU - Schneider, Rainer

AU - Katinger, Hermann

AU - Andó, I.

AU - Dierich, Manfred P.

PY - 1997

Y1 - 1997

N2 - Adhesion molecules are known to contribute to infectivity of HIV-1. Here we tested whether the complement receptor type 3 (CR3, CD11b), an α(m)β2 integrin, plays an accessory role in the infection process of HIV-1, because ICAM-1, a ligand of CR3, is present on the envelope of HIV-1. In addition, the vital transmembrane protein gp41 shares four regions of homology with the complement component C3, a further CR3 ligand. Infection of PBMCs with HIV- IIIB and primary isolates was partially inhibited by anti-CR3 antibodies. A peptide derived from the complement component C3, covering the CR3-binding site of C3 and sharing strong similarity to the immunosuppressive region of gp41, significantly reduced the HIV-1 titer in infection assays. Recombinant soluble gp41 (rsgp41) and the peptide covering the immunosuppressive domain of gp41 inhibited the rosetting of iC3b-coated sheep erythrocytes with U937 via complement receptors (CRs) with an efficiency comparable to monoclonal anti-CR antibodies. In addition, sub-populations of CD4 + and CD8 + T-cells isolated from HIV-infected individuals were found to upregulate CR3 as determined by FACS analysis and on the mRNA level. Since gp41 has been implicated in viral fusion, an interaction of its C3-homology region in gp41 or an interaction of ICAM on the surface of free virus with CRs might contribute to facilitate viral entry.

AB - Adhesion molecules are known to contribute to infectivity of HIV-1. Here we tested whether the complement receptor type 3 (CR3, CD11b), an α(m)β2 integrin, plays an accessory role in the infection process of HIV-1, because ICAM-1, a ligand of CR3, is present on the envelope of HIV-1. In addition, the vital transmembrane protein gp41 shares four regions of homology with the complement component C3, a further CR3 ligand. Infection of PBMCs with HIV- IIIB and primary isolates was partially inhibited by anti-CR3 antibodies. A peptide derived from the complement component C3, covering the CR3-binding site of C3 and sharing strong similarity to the immunosuppressive region of gp41, significantly reduced the HIV-1 titer in infection assays. Recombinant soluble gp41 (rsgp41) and the peptide covering the immunosuppressive domain of gp41 inhibited the rosetting of iC3b-coated sheep erythrocytes with U937 via complement receptors (CRs) with an efficiency comparable to monoclonal anti-CR antibodies. In addition, sub-populations of CD4 + and CD8 + T-cells isolated from HIV-infected individuals were found to upregulate CR3 as determined by FACS analysis and on the mRNA level. Since gp41 has been implicated in viral fusion, an interaction of its C3-homology region in gp41 or an interaction of ICAM on the surface of free virus with CRs might contribute to facilitate viral entry.

KW - Adhesion molecule

KW - CR3

KW - gp41

KW - HIV

UR - http://www.scopus.com/inward/record.url?scp=0031414824&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031414824&partnerID=8YFLogxK

U2 - 10.1016/S0161-5890(97)00108-9

DO - 10.1016/S0161-5890(97)00108-9

M3 - Article

VL - 34

SP - 855

EP - 863

JO - Molecular Immunology

JF - Molecular Immunology

SN - 0161-5890

IS - 12-13

ER -