Results 131 to 140 of about 4,355,851 (162)

The complex antigenicity of a small external region of theC-terminal tail of the HIV-1 gp41 envelope protein: a lesson in epitope analysis

Reviews in Medical Virology, 2005
The newly discovered external tail loop within the C-terminal tail of the gp41 transmembrane subunit of the HIV-1 envelope protein comprises approximately 40 residues, and within this are 18-residues ((734)PDRPEGIEEEGGERDRDR(751)) that include three antibody-reactive regions.
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Interaction of several complement proteins with gp120 and gp41, the two envelope gycoproteins of HIV-1

AIDS, 1995
To study the binding of human complement proteins to gp41 and gp120 of HIV-1.The interaction of complement proteins with gp41 and gp120 and their effect on the gp41-gp120 complex in enzyme-linked immunosorbent assays (ELISA) and on stably transfected Schneider-2 cells expressing a gp41-gp120 complex was investigated.
H, Stoiber, C, Ebenbichler, R, Schneider, J, Janatova, M P, Dierich   +4 more
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Antibody-dependent cellular cytotoxicity is directed against both the gp120 and gp41 envelope proteins of HIV

Aids, 1989
To define the target antigens for antibody-dependent cellular cytotoxicity (ADCC), assays were performed using affinity-purified human immunoglobulin (Ig) or polyclonal rabbit sera directed against specific proteins of HIV. ADCC was not found using affinity-purified anti-core (p25) human Ig or sera obtained from rabbits hyper-immunized with recombinant
L A, Evans, G, Thomson-Honnebier, K, Steimer, E, Paoletti, M E, Perkus, H, Hollander, J A, Levy   +6 more
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Theoretically Determined Three-Dimensional Structures for Amphipathic Segments of the HIV-1 gp41 Envelope Protein

AIDS Research and Human Retroviruses, 1989
Three-dimensional computer models for two segments of the C terminus of gp41, the transmembrane AIDS envelope protein, which may form amphipathic α-helices, have been generated using structure prediction techniques combined with energy minimization and molecular dynamics simulations.
R M, Venable, R W, Pastor, B R, Brooks, F W, Carson   +3 more
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The immunosuppressive domain of the transmembrane envelope protein gp41 of HIV-1 binds to human monocytes and B cells

Immunologic Research, 2016
The induction of the acquired immunodeficiency syndrome by the human immunodeficiency virus-1 (HIV-1) is a complex process which is not yet understood in full detail. Still open is the question whether the highly conserved so-called immunosuppressive (Isu) domain in the transmembrane envelope (TM) protein gp41 of HIV-1 is actively participating in ...
Michael, Mühle, Tobias, Kroniger, Kerstin, Hoffmann, Joachim, Denner   +3 more
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HIV-1 envelope protein gp41 modulates expression of interleukin-10 and chemokine receptors on monocytes, astrocytes and neurones

AIDS, 2000
To analyse the effect of HIV-1 transmembrane protein gp41 on cytokine production and chemokine receptor expression in blood and brain.Because previous results had demonstrated that recombinant gp41 contributes to HIV-induced dysfunction of blood immune cells we investigated its effect on interleukin (IL)-10 synthesis and expression of the HIV ...
C, Speth, B, Joebstl, M, Barcova, M P, Dierich   +3 more
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[Towards a vaccine for HIV infection: role of the gp41 envelope protein].

Bulletin de l'Academie nationale de medecine, 2009
HIV infection leads to a gradual deterioration in immune status. The mechanisms underlying CD4 T cell depletion in this setting are controversial. One of the most intriguing phenomena is that many uninfected CD4 cells die prematurely in HIV-infected subjects. We therefore investigated the possibility that these cells are killed by a collateral effector
Patrice, Debre, Dominique, Costagliola, Roger, Legrand, Vincent, Vieillard   +3 more
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Interaction of a basic amphipathic peptide from the carboxyterminal part of the HIV envelope protein gp41 with negatively charged lipid surfaces

Chemistry and Physics of Lipids, 1998
The interaction of the positively charged synthetic amphipathic peptide fragment gp41(828) corresponding to a segment from the carboxyterminal region of the HIV envelope glycoprotein gp41 with lipid monolayers spread at the air-water interface has been studied by film balance measurements.
D, Trommeshauser, H J, Galla
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Class I-restricted presentation of an HIV-1 gp41 epitope containing an N-linked glycosylation site. Implications for the mechanism of processing of viral envelope proteins

The Journal of Immunology, 1996
Abstract Uncertainty exists over the site of processing of viral envelope (env) proteins for recognition by CTL. The extracellular domains of env proteins are not present in the cytosol, the site where the class I Ag processing pathway begins.
R L, Ferris, C, Buck, S A, Hammond, A S, Woods, R J, Cotter, M, Takiguchi, Y, Igarashi, Y, Ichikawa, R F, Siliciano   +8 more
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The effect of lipid composition and physical state of phospholipid monolayer on the binding and incorporation of a basic amphipathic peptide from the C-terminal region of the HIV envelope protein gp41

Chemistry and Physics of Lipids, 2000
The interaction of a peptide identical to the carboxy terminal region of the envelope glycoprotein gp41(828) of HIV with negatively charged phospholipids in a monolayer was studied by a Wilhelmy film balance. No significant interaction of the peptide with a monolayer composed of pure neutral but a strong affinity to negatively charged phospholipids ...
D, Trommeshauser, S, Krol, L D, Bergelson, H J, Galla   +3 more
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