scholarly journals Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino acid sequence of the viral envelope, gp120.

1988 ◽  
Vol 85 (9) ◽  
pp. 3198-3202 ◽  
Author(s):  
J. R. Rusche ◽  
K. Javaherian ◽  
C. McDanal ◽  
J. Petro ◽  
D. L. Lynn ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Viral Envelope ◽  
Immunodeficiency Virus ◽  
Infected Cells ◽  
Envelope Gp120

scholarly journals Reversion of a Human Immunodeficiency Virus Type 1 Matrix Mutation Affecting Gag Membrane Binding, Endogenous Reverse Transcriptase Activity, and Virus Infectivity

1999 ◽  
Vol 73 (6) ◽  
pp. 4728-4737 ◽  
Author(s):  
Rosemary E. Kiernan ◽  
Akira Ono ◽  
Eric O. Freed
Keyword(s):  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Reverse Transcriptase ◽  
Reverse Transcriptase Activity ◽  
Wild Type ◽  
Viral Dna ◽  
Transcriptase Activity ◽  
Immunodeficiency Virus ◽  
Infected Cells

ABSTRACT We previously characterized mutations in the human immunodeficiency virus type 1 matrix (MA) protein that displayed reduced infectivity in single-round assays, defects in the stable synthesis of viral DNA in infected cells, and impaired endogenous reverse transcriptase activity. The mutants, which contained substitutions in a highly conserved Leu at MA amino acid 20, also increased binding of Gag to membrane. To elucidate further the role of MA in the virus replication cycle, we have characterized a viral revertant of an amino acid 20 mutant (20LK). The revertant virus, which replicates with essentially wild-type kinetics in H9 cells, contains second-site compensatory changes at MA amino acids 73 (E→K) and 82 (A→T), while retaining the original 20LK mutation. Single-cycle infectivity assays, performed with luciferase-expressing viruses, show that the 20LK/73EK/82AT triple mutant displays markedly improved infectivity relative to the original 20LK mutant. The stable synthesis of viral DNA in infected cells is also significantly increased compared with that of 20LK DNA. Furthermore, activity of revertant virions in endogenous reverse transcriptase assays is restored to near-wild-type-levels. Interestingly, although 20LK/73EK/82AT reverses the defects in replication kinetics, postentry events, and endogenous reverse transcriptase activity induced by the 20LK mutation, the reversion does not affect the 20LK-imposed increase in Gag membrane binding. Mutants containing single and double amino acid substitutions were constructed, and their growth kinetics were examined. Only virus containing all three changes (20LK/73EK/82AT) grew with significantly accelerated kinetics; 73EK, 73EK/82AT, and 20LK/82AT mutants displayed pronounced defects in virus particle production. Viral core-like complexes were isolated by sucrose density gradient centrifugation of detergent-treated virions. Intriguingly, the protein composition of wild-type and mutant detergent-resistant complexes differed markedly. In wild-type and 20LK complexes, MA was removed following detergent solubilization of the viral membrane. In contrast, in revertant preparations, the majority of MA cosedimented with the detergent-resistant complex. These results suggest that the 20LK/73EK/82AT mutations induced a significant alteration in MA-MA or MA-core interactions.

scholarly journals Cell surface effects of human immunodeficiency virus

1988 ◽  
Vol 8 (1) ◽  
pp. 35-48 ◽  
Author(s):  
Robert F. Garry ◽  
A. Arthur Gottlieb ◽  
Kenneth P. Zuckerman ◽  
John R. Pace ◽  
Thomas W. Frank ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Cell Surface ◽  
Cell Fusion ◽  
Surface Effects ◽  
Cell Killing ◽  
Viral Envelope ◽  
Rational Approach ◽  
Immunodeficiency Virus ◽  
Infected Cells ◽  
Cell Cell

Cell killing by human immunodeficiency virus (HIV) is thought to contribute to many of the defects of the acquired immunodeficiency syndrome (AIDS). Two types of cytopathology are observed in HIV-infected cultured cells: cell-cell fusion and killing of single cells. Both killing processes appear to involve cell surface effects of HIV. A model is proposed for the HIV-mediated cell surface processes which could result in cell-cell fusion and single cell killing. The purpose of this model is to define the potential roles of individual viral envelope and cell surface molecules in cell killing processes and to identify alternative routes to the establishment of persistently-infected cells. Elucidation of HIV-induced cell surface effects may provide the basis for a rational approach to the design of antiviral agents which are selective for HIV-infected cells.

A Serologic Analysis and the Amino Acid Sequence of the V3 Region of Human Immunodeficiency Virus from Carriers in Bangkok

1994 ◽  
Vol 169 (1) ◽  
pp. 227-228 ◽  
Author(s):  
K. Okuda ◽  
H. Bukawa ◽  
S. Kawamoto ◽  
M. Imai ◽  
T. Saito ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Immunodeficiency Virus ◽  
V3 Region

Antibodies from Human Immunodeficiency Virus-Infected Individuals Bind to a Short Amino Acid Sequence that Elicits Neutralizing Antibodies in Animals

1989 ◽  
Vol 5 (2) ◽  
pp. 173-182 ◽  
Author(s):  
WILLIAM R. KENEALY ◽  
THOMAS J. MATTHEWS ◽  
MONG-CHING GANFIELD ◽  
ALPHONSE J. LANGLOIS ◽  
DAVID M. WASELEFSKY ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neutralizing Antibodies ◽  
Immunodeficiency Virus ◽  
Short Amino Acid Sequence

scholarly journals Antibody-Producing Effects in Mice by Synthetic Immunoactive Lipopeptides with the Conjugated Amino Acid Sequence of gp120 in Human Immunodeficiency Virus.

1996 ◽  
Vol 19 (10) ◽  
pp. 1271-1274 ◽  
Author(s):  
Tadayori SHIMIZU ◽  
Yoshihisa IWAMOTO ◽  
Yasutake YANAGIHARA ◽  
Kazuo RYOYAMA ◽  
Yasufumi MARUYAMA ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Immunodeficiency Virus

scholarly journals Frequent Detection of Escape from Cytotoxic T-Lymphocyte Recognition in Perinatal Human Immunodeficiency Virus (HIV) Type 1 Transmission: the Ariel Project for the Prevention of Transmission of HIV from Mother to Infant

1999 ◽  
Vol 73 (5) ◽  
pp. 3975-3985 ◽  
Author(s):  
Cara C. Wilson ◽  
R. Clark Brown ◽  
Bette T. Korber ◽  
Barbara M. Wilkes ◽  
Debbie J. Ruhl ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Variation ◽  
Amino Acid Sequence Variation ◽  
Immunodeficiency Virus ◽  
Immunologic Factors ◽  
Hiv Type 1 ◽  
Hiv 1

ABSTRACT Host immunologic factors, including human immunodeficiency virus (HIV)-specific cytotoxic T lymphocytes (CTL), are thought to contribute to the control of HIV type 1 (HIV-1) replication and thus delay disease progression in infected individuals. Host immunologic factors are also likely to influence perinatal transmission of HIV-1 from infected mother to infant. In this study, the potential role of CTL in modulating HIV-1 transmission from mother to infant was examined in 11 HIV-1-infected mothers, 3 of whom transmitted virus to their offspring. Frequencies of HIV-1-specific human leukocyte antigen class I-restricted CTL responses and viral epitope amino acid sequence variation were determined in the mothers and their infected infants. Maternal HIV-1-specific CTL clones were derived from each of the HIV-1-infected pregnant women. Amino acid substitutions within the targeted CTL epitopes were more frequently identified in transmitting mothers than in nontransmitting mothers, and immune escape from CTL recognition was detected in all three transmitting mothers but in only one of eight nontransmitting mothers. The majority of viral sequences obtained from the HIV-1-infected infant blood samples were susceptible to maternal CTL. These findings demonstrate that epitope amino acid sequence variation and escape from CTL recognition occur more frequently in mothers that transmit HIV-1 to their infants than in those who do not. However, the transmitted virus can be a CTL susceptible form, suggesting inadequate in vivo immune control.

Sign in / Sign up

Export Citation Format

Share Document