Neutralizing Antibody to the AIDS Virus Prevalence, Clinical Significance and Virus Strain Specificity1

2015 ◽  
pp. 151-158 ◽  
Author(s):  
Alfred M. Prince ◽  
Donna Pascual ◽  
Luda Bardina-Kosolopov ◽  
Dean Kurokawa ◽  
Louis Baker ◽  
...  
Keyword(s):  
Clinical Significance ◽  
Virus Strain ◽  
Neutralizing Antibody ◽  
Virus Prevalence ◽  
Aids Virus

scholarly journals Enhanced Virulence Mediated by the Murine Coronavirus, Mouse Hepatitis Virus Strain JHM, Is Associated with a Glycine at Residue 310 of the Spike Glycoprotein

2003 ◽  
Vol 77 (19) ◽  
pp. 10260-10269 ◽  
Author(s):  
Evelena Ontiveros ◽  
Taeg S. Kim ◽  
Thomas M. Gallagher ◽  
Stanley Perlman
Keyword(s):  
Virus Strain ◽  
Hepatitis Virus ◽  
Neurological Diseases ◽  
Mouse Hepatitis Virus ◽  
Neutralizing Antibody ◽  
Lateral Spread ◽  
S Protein ◽  
Acute Encephalitis ◽  
The Central Nervous System

ABSTRACT The coronavirus, mouse hepatitis virus strain JHM, causes acute and chronic neurological diseases in rodents. Here we demonstrate that two closely related virus variants, both of which cause acute encephalitis in susceptible strains of mice, cause markedly different diseases if mice are protected with a suboptimal amount of an anti-JHM neutralizing antibody. One strain, JHM.SD, caused acute encephalitis, while infection with JHM.IA resulted in no acute disease. Using recombinant virus technology, we found that the differences between the two viruses mapped to the spike (S) glycoprotein and that the two S proteins differed at four amino acids. By engineering viruses that differed by only one amino acid, we identified a serine-to-glycine change at position 310 of the S protein (S310G) that recapitulated the more neurovirulent phenotype. The increased neurovirulence mediated by the virus encoding glycine at position S310 was not associated with a different tropism within the central nervous system (CNS) but was associated with increased lateral spread in the CNS, leading to significantly higher brain viral titers. In vitro studies revealed that S310G was associated with decreased S1-S2 stability and with enhanced ability to mediate infection of cells lacking the primary receptor for JHM (“receptor-independent spread”). These enhanced fusogenic properties of viruses encoding a glycine at position 310 of the S protein may contribute to spread within the CNS, a tissue in which expression of conventional JHM receptors is low.

scholarly journals Coronavirus antibody titres in sera of healthy adults and experimentally infected volunteers

1972 ◽  
Vol 70 (2) ◽  
pp. 235-244 ◽  
Author(s):  
A. F. Bradburne ◽  
B. A. Somerset
Keyword(s):  
General Population ◽  
Virus Strain ◽  
High Frequency ◽  
Haemagglutination Inhibition ◽  
Neutralizing Antibody ◽  
Antibody Responses ◽  
Normal Adult ◽  
Apparent Increase ◽  
Antibody Titres ◽  
Heterologous Antibody

SUMMARYSix coronaviruses isolated in the U.S.A. have been inoculated into volunteers and all produced colds. Between 10 and 20 % of infected volunteers developed heterologous antibody responses after these and other experimental infections with coronaviruses. The haemagglutination-inhibition test with the OC43 virus strain was found to detect antibody rises after infection with a variety of strains.Studies on normal adult sera taken between 1965 and 1970 revealed a high frequency of neutralizing antibody to one strain (229E) and a frequency of HI antibody to strain OC43 which fluctuated from year to year. Complement-fixing antibodies to these two viruses were also found, revealing an apparent increase in the activity of coronaviruses in the general population of the U.K., during the winter of 1968–9.

scholarly journals Prevention of Disease Induced by a Partially Heterologous AIDS Virus in Rhesus Monkeys by Using an Adjuvanted Multicomponent Protein Vaccine

2003 ◽  
Vol 77 (2) ◽  
pp. 1049-1058 ◽  
Author(s):  
Gerald Voss ◽  
Kelledy Manson ◽  
David Montefiori ◽  
David I. Watkins ◽  
Jonathan Heeney ◽  
...  
Keyword(s):  
Rhesus Monkeys ◽  
Neutralizing Antibody ◽  
Protein Vaccine ◽  
Structural Protein ◽  
Protein Subunit ◽  
Virus Envelope ◽  
Immunodeficiency Virus ◽  
Aids Virus ◽  
Aids Vaccines ◽  
Virus Envelope Protein

ABSTRACT Recombinant protein subunit AIDS vaccines have been based predominantly on the virus envelope protein. Such vaccines elicit neutralizing antibody responses that can provide type-specific sterilizing immunity, but in most cases do not confer protection against divergent viruses. In this report we demonstrate that a multiantigen subunit protein vaccine was able to prevent the development of disease induced in rhesus monkeys by a partially heterologous AIDS virus. The vaccine was composed of recombinant human immunodeficiency virus type 1 (HIV-1) gp120, NefTat fusion protein, and simian immunodeficiency virus (SIV) Nef formulated in the clinically tested adjuvant AS02A. Upon challenge of genetically unselected rhesus monkeys with the highly pathogenic and partially heterologous SIV/HIV strain SHIV89.6p the vaccine was able to reduce virus load and protect the animals from a decline in CD4-positive cells. Furthermore, vaccination prevented the development of AIDS for more than 2.5 years. The combination of the regulatory proteins Nef and Tat together with the structural protein gp120 was required for vaccine efficacy.

Enhancing neutralizing antibody production by an interferon-inducing porcine reproductive and respiratory syndrome virus strain

Vaccine ◽  
2013 ◽  
Vol 31 (47) ◽  
pp. 5537-5543 ◽  
Author(s):  
Rong Wang ◽  
Yueqiang Xiao ◽  
Tanja Opriessnig ◽  
Yi Ding ◽  
Ying Yu ◽  
...  
Keyword(s):  
Virus Strain ◽  
Antibody Production ◽  
Neutralizing Antibody ◽  
Respiratory Syndrome Virus

Prevalence, Clinical Significance, and Straln Specificity of Neutralizing Antibody to the Human Immunodeficiency Virus

1987 ◽  
Vol 156 (2) ◽  
pp. 268-272 ◽  
Author(s):  
A. M. Prince ◽  
D. Pascual ◽  
L. B. Kosolapov ◽  
D. Kurokawa ◽  
L. Baker ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Clinical Significance ◽  
Neutralizing Antibody ◽  
Immunodeficiency Virus

Presence of antibody in virus-infected brain cells of SSPE ferrets

1983 ◽  
Vol 41 ◽  
pp. 804-805
Author(s):  
Hannah R. Brown ◽  
Tammy L. Donato ◽  
Halldor Thormar
Keyword(s):  
Measles Virus ◽  
Plasma Cells ◽  
Subacute Sclerosing Panencephalitis ◽  
Protein A ◽  
Neutralizing Antibody ◽  
Brain Cells ◽  
Antibody Titers ◽  
A Cell ◽  
The Central Nervous System ◽  
The Brain

Measles virus specific immunoglobulin G (IgG) has been found in the brains of patients with subacute sclerosing panencephalitis (SSPE), a slowly progressing disease of the central nervous system (CNS) in children. IgG/albumin ratios indicate that the antibodies are synthesized within the CNS. Using the ferret as an animal model to study the disease, we have been attempting to localize the Ig's in the brains of animals inoculated with a cell associated strain of SSPE. In an earlier report, preliminary results using Protein A conjugated to horseradish peroxidase (PrAPx) (Dynatech Diagnostics Inc., South Windham, ME.) to detect antibodies revealed the presence of immunoglobulin mainly in antibody-producing plasma cells in inflammatory lesions and not in infected brain cells.In the present experiment we studied the brain of an SSPE ferret with neutralizing antibody titers of 1:1024 in serum and 1:512 in CSF at time of sacrifice 7 months after i.c. inoculation with SSPE measles virus-infected cells. The animal was perfused with saline and portions of the brain and spinal cord were immersed in periodate-lysine-paraformaldehyde (P-L-P) fixative. The ferret was not perfused with fixative because parts of the brain were used for virus isolation.

Clinical significance of cathepsin E in pancreatic juice in the diagnosis of pancreatic ductal adenocarcinoma

2000 ◽  
Vol 15 (11) ◽  
pp. 1333-1338 ◽  
Author(s):  
Koji Uno ◽  
Takeshi Azuma ◽  
Masatsugu Nakajima ◽  
Kenjiro Yasuda ◽  
Takanobu Hayakumo ◽  
...  
Keyword(s):  
Pancreatic Ductal Adenocarcinoma ◽  
Clinical Significance ◽  
Pancreatic Juice ◽  
Ductal Adenocarcinoma ◽  
Cathepsin E
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