Pathogenesis of Human Immunodeficiency Virus Infection

Levy, Jay A.

doi:10.1111/j.1749-6632.1989.tb16459.x

Cited by 222 publications

(303 citation statements)

References 516 publications

(848 reference statements)

Supporting

Mentioning

290

Contrasting

Unclassified

Order By: Relevance

“…Treatment with RT inhibitors favors the emergence of drug-resistant HIV strains. V3-derived SPCs such as [GPGRAF]8-SPC appear to be a promising alternative approach for limiting the dissemination of viral infection in HIV-infected people, which may occur primarily through cell-to-cell contacts (20).…”

Section: Inhibition Of Hiv-1 and Hiv-2 Infection Ofmentioning

confidence: 99%

“…The development of vaccines and immunotherapy for HIV is therefore difficult (4). The V3 loop of HIV-1 gpl20 does not seem to be involved in the binding of gpl20 to its main cellular receptor, CD4, a 55-kDa glycoprotein on the surface of a subclass of T lymphocytes and on macrophages (20). Nevertheless, several studies indicate that the V3 loop may be involved in the postbinding events necessary for viral entry into the cells (14,25).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Multibranched V3 peptides inhibit human immunodeficiency virus infection in human lymphocytes and macrophages

Yahi¹,

Fantini²,

Mabrouk³

et al. 1995

Peptides 1994

View full text Add to dashboard Cite

Section: Inhibition Of Hiv-1 and Hiv-2 Infection Ofmentioning

confidence: 99%

mentioning

confidence: 99%

Multibranched V3 peptides inhibit human immunodeficiency virus infection in human lymphocytes and macrophages

Yahi¹,

Fantini²,

Mabrouk³

et al. 1995

Peptides 1994

View full text Add to dashboard Cite

“…Both the fusion of the viral and target CD4 + cell membranes and the fusion of HIV-infected cells with CD4 + cells is a pH-independent process, and is preceded by the binding of the viral envelope glycoprotein gpl20 to CD4 (Lifson et al, 1986;Sodroski et al, 1986;Sinangil et al, 1988;Stein & Engleman, 1991;Levy, 1993). The mechanism of this fusion reaction is an area of active investigation.…”

Section: Introductionmentioning

confidence: 99%

“…Human immunodeficiency virus type 1 (HIV-1) predominantly utilizes the T cell surface antigen CD4 as a receptor for infection of susceptible cells (reviewed in Levy, 1993). Both the fusion of the viral and target CD4 + cell membranes and the fusion of HIV-infected cells with CD4 + cells is a pH-independent process, and is preceded by the binding of the viral envelope glycoprotein gpl20 to CD4 (Lifson et al, 1986;Sodroski et al, 1986;Sinangil et al, 1988;Stein & Engleman, 1991;Levy, 1993).…”

Section: Introductionmentioning

confidence: 99%

A monoclonal antibody to the gp120-CD4 complex has differential effects on HIV-induced syncytium formation and viral infectivity

Konopka

Pretzer²,

Celada³

et al. 1995

Journal of General Virology

View full text Add to dashboard Cite

A murine monoclonal antibody (MAb F-91-55) raised against the complex of soluble CD4 and human immunodeficiency virus type 1 (HIV-1) gpl20 had previously been found to inhibit syncytium formation without inhibiting the interaction of CD4 with gpl20, and its binding site was localized within the first two domains (D 1/D2) of CD4. We investigated whether this antibody inhibited the infectivity of HIV-1 in the CD4 + T cell lines A3.01, Sup-T1 and H9. We also examined the effect of the antibody on syncytium formation between these cells and chronically infected H9 cells. Syncytium formation was found to depend critically on the incubation medium used. The effect of the MAb on HIV-1 infectivity was very limited with A3.01 and Sup-TI cells, although it inhibited syncytium formation between A3.01 or Sup-T1 and chronically infected H9 cells. In contrast, the MAb inhibited significantly the infectivity of HIV-1 in H9 cells, but it also inhibited syncytium formation between H9 and chronically infected H9 cells to a greater extent than in the case of the other cell lines. Our results indicate that cellular systems used for syncytium assays differ in their susceptibility to inhibitory antibodies. In the A3.01 and Sup-T1 cell systems, the differences in the ability of the MAb to block viral entry or syncytium formation raise the possibility that the mechanisms of interaction of gp 120/ gp41 with cell membrane CD4 may be different in cell-cell and virus-cell membrane fusion.

show abstract

“…This chapter summerizes only the major steps in the viral life cycle (for further details see Levy, 1993). In permissive activated T cells, HIV-1 undergoes integration and replication within 24 h after infection (Kim etal., 1990).…”

Section: Overview Of the Hiv-1 Life Cyclementioning

confidence: 99%

Review

1996

Biological Chemistry Hoppe-Seyler

View full text Add to dashboard Cite

Proteolytic enzymes have many physiological functions in plants, bacteria, viruses, protozoa and mammals. They play a role in processes such as food digestion, complement activation or blood coagulation. The action of proteolytic enzymes is biologically controlled by proteinase inhibitors and increasing attention is being paid to the physiological significance of these natural inhibitors in pathological processes. The reason for this growing interest is that uncontrolled proteolysis can lead to irreversible damage e.g. in chronic inflammation or tumor metastasis. This review focusses on the possible role of the cystatins, natural and specific inhibitors of the cysteine proteinases, in pathological processes. Key words: Cystatins / Cysteine proteinases / Inflammation / Inhibitors / Pathological processes. Cysteine ProteinasesCysteine Proteinases, synonymous with thiol proteinases, are small proteins with molecular masses varying from 23 to 24 kDa and with two catalytic residues, Cys25 and His159, which are involved in the hydrolytic reaction. Cysteine proteinases catalyze the hydrolysis of various polypeptide substrates and are most active under reducing and mildly acidic conditions (pH 5 -6.5). They have been detected in and isolated from a large number of biological sources including plants, bacteria, animals and humans. Bacterial cysteine proteinases are produced by Clostridium histolyticum, named clostripain, by hemolytic group A streptococci and by the pathogenic anaerobic Porphyromonas gingivalis, a bacterium associated with periodontitis. Bacterial cysteine proteinases probably play a role in the penetration of normal tissues by the bacteria and in the food digestion. Viral cysteine proteinases from picornaviruses, e.g. the poliovirus and rhinovirus type I, are involved in proteolytic cleavage of precursor proteins for virus replication and for the production of new virus particles. A virus-coded cysteine proteinase is involved in this process (Kay and Dunn, 1990; Körant et a/., 1985;. HIV-I also needs proteolytic processing by cysteine proteinases to regulate the expression of viral proteins (Guy ef a/., 1991). Protozoal cysteine proteinases are produced by a number of protozoan parasites to facilitate host invasion, metabolize host proteins, to degrade the host immune molecules or to use them for intracellular replication. Cysteine proteinases are produced by e.g. Trypanosoma cruzi, the causative agent of American trypanosomiasis or by Leishmania species, causing one of the six major parasitic diseases. Furthermore, human malarial parasites produce a broad scala of proteinases including cysteine proteinase which are involved in erythrocyte invasion and rupture (McKerrow, 1993). Mammalian cysteine proteinases are present in the lysosomes of cells. Lysosomes contain different cysteine proteinases, the most important being the cathepsins B, H, L and S Kirschke, 1981, Barrett et a/., 1988). These cathepsins have common ancestors and are related to papain. Cathepsin B has been detected in every tissue or cel...

show abstract

Pathogenesis of Human Immunodeficiency Virus Infection

Cited by 222 publications

References 516 publications

Multibranched V3 peptides inhibit human immunodeficiency virus infection in human lymphocytes and macrophages

Multibranched V3 peptides inhibit human immunodeficiency virus infection in human lymphocytes and macrophages

A monoclonal antibody to the gp120-CD4 complex has differential effects on HIV-induced syncytium formation and viral infectivity

Review

Contact Info

Product

Resources

About