Ann R. Hunt

Colorado State University

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John T. Roehrig

Centers for Disease Control and Prevention

Gwong‐Jen J. Chang

Centers for Disease Control and Prevention

James H. Mathews

Centers for Disease Control and Prevention

Alison J. Johnson

Albert Einstein College of Medicine

Richard A. Bolin

United States Department of Health and Human Services

Carol D. Blair

Colorado State University

Brent S. Davis

Centers for Disease Control and Prevention

Shana Frederickson

Alexion Pharmaceuticals (United States)

Kristy L. Gottfried

Centers for Disease Control and Prevention

Derek A Holmes

Genentech

Cooperative Institutions

Centers for Disease Control and Prevention

United States Department of Health and Human Services

National Center for Infectious Diseases

Colorado State University

National Center for Emerging and Zoonotic Infectious Diseases

Vector (United States)

Kenya Medical Research Institute

National Institutes of Health

The University of Texas Medical Branch at Galveston

Johns Hopkins University

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A recombinant particulate antigen of Japanese encephalitis virus produced in stably-transformed cells is an effective noninfectious antigen and subunit immunogen

Journal of Virological Methods (2001)

Ann R. Hunt C. B. Cropp Gwong‐Jen J. Chang

Immunogen

Virus-like particle

10.1016/s0166-0934(01)00346-9

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Citations (79)

Flavivirus DNA Vaccines

Annals of the New York Academy of Sciences (2001)

Gwong‐Jen J. Chang Brent S. Davis Ann R. Hunt Derek A Holmes Goro Kuno

A bstract : The use of DNA‐based vaccines is a novel and promising immunization approach for the development of flavivirus vaccines. This approach has been attempted in vaccine development for various virus species, including St. Louis encephalitis, Russian spring‐summer encephalitis, Central European encephalitis, dengue serotypes 1 and 2, Murray Valley encephalitis, Japanese encephalitis, and West Nile viruses. However, very little is known about the factors affecting its efficacy. Recently, we demonstrated that a single intramuscular immunization of DNA vaccine of Japanese encephalitis and West Nile viruses protected mice and horses from virus challenge. Administration of these recombinant plasmid vectors resulted in endogenous expression and secretion of extracellular virus‐like particles that correlated well with the induction of protective immunity. These results provided evidence that the virus‐like particles composed of premembrane/membrane and envelope proteins are essential for eliciting immune responses similar to those induced by live, attenuated virus vaccines. The biosynthesis and protein processing of premembrane/membrane and envelope proteins that preserve the native conformation and glycosylation profiles identical to virion proteins could be determined by the effectiveness of the transmembrane signal sequence located at the amino‐terminus of premembrane protein. The use of DNA vaccines in multivalent and/or combination vaccines designed to immunize against multiple flaviviruses is also a promising area of development.

Flavivirus

Dengue vaccine

10.1111/j.1749-6632.2001.tb02703.x

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Citations (58)

Antigenic Structure of the Murray Valley Encephalitis Virus E Glycoprotein

Journal of General Virology (1988)

R. A. Hawkes John T. Roehrig Ann R. Hunt Gloria A. Moore

Summary To complement our battery of St Louis encephalitis (SLE) virus monoclonal antibodies (MAbs), we isolated and characterized MAbs reactive with another member of the SLE virus serocomplex, Murray Valley encephalitis (MVE) virus. From 40 fusion products, we isolated 10 stable hybridomas. The combination of SLE and MVE virus MAbs defined eight epitopes on the MVE envelope (E) glycoprotein. Six of these epitopes (E-1a, E-1c, E-1d, E-3, E-4a, E-4b) were identical to those previously demonstrated on SLE virus. Two new epitopes (E-5 and E-6) were also identified. As with SLE virus, the MVE E-1c epitope elicited the most potent virus-neutralizing and protective MAb. Unlike SLE virus, however, one of the cross-reactive epitopes (E-5) elicited neutralizing antibody and protected animals from MVE virus challenge. These results indicate that, while the antigenic domains on viruses within the SLE virus serocomplex are quite similar, epitopes involved in virus neutralization or protection from virus challenge may vary and can be topologically distinct.

10.1099/0022-1317-69-5-1105

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Citations (37)

T-Helper Cell Epitopes on the E-Glycoprotein of Dengue 2 Jamaica Virus

Virology (1994)

John T. Roehrig Peggy Risi John R. Brubaker Ann R. Hunt Barry J. Beaty

10.1006/viro.1994.1005

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Citations (57)

Synthetic peptides of venezuelan equine encephalomyelitis virus E2 glycoprotein. III. Identification of a protective peptide derived from the carboxy-terminal extramembranal one-third of the protein

Virology (1991)

Alison J. Johnson Ann R. Hunt John T. Roehrig

Encephalomyelitis

10.1016/0042-6822(91)90555-p

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Citations (9)

Arbovirus Investigations in Argentina, 1977–1980

American Journal of Tropical Medicine and Hygiene (1985)

C. H. Calisher T. P. Monath M. S. Sabattini J. Kerschner C. J. Mitchell

Forty viruses isolated from mosquitoes between 1977 and 1980 in Argentina have been identified and characterized. Nineteen strains of VEE virus, identical by neutralization (N) tests, were shown by hemagglutination-inhibition tests with anti-E2 glycoprotein sera to represent a new subtype VI of the VEE complex. RNA oligonucleotide fingerprints of this virus were distinct from subtype I viruses. The virus was not lethal for English short-haired guinea pigs, indicating that it is probably not equine-virulent. Three strains of a member of the WEE virus complex were shown to differ by N tests in 1 direction from prototype WEE virus. The new WEE subtype was also found to be distinct by RNA oligonucleotide mapping. Its vector relationships indicate that it is an enzootic virus, and it has not been associated with equine disease. A new member of the Anopheles A serogroup was identified, shown to be most closely related to Lukuni and Col An 57389 viruses, and given the name Las Maloyas virus. A strain of Para virus (Bunyaviridae, Bunyavirus) was identified. Six isolates, representing 3 new viruses morphologically resembling bunyaviruses are described; the names Antequera, Barranqueras, and Resistencia are proposed for these agents, which were all isolated from Culex (Melanoconion) delpontei in Chaco Province. No serologic relationships between these viruses and other bunyaviruses were found. Since they are antigenically interrelated, they form a new (Antequera) serogroup. Eight Gamboa serogroup viruses and 2 strains of St. Louis encephalitis virus were also identified.

Enzootic

Orbivirus

Encephalitis Viruses

Togaviridae

10.4269/ajtmh.1985.34.956

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Citations (26)

Selection and Partial Characterization of Dengue 2 Virus Mutants That Induce Fusion at Elevated pH

Virology (1993)

Farshad Guirakhoo Ann R. Hunt Joyce G. Lewis John T. Roehrig

Aedes albopictus

10.1006/viro.1993.1252

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Citations (98)

Localization of a protective epitope on a Venezuelan equine encephalomyelitis (VEE) virus peptide that protects mice from both epizootic and enzootic VEE virus challenge and is immunogenic in horses

Vaccine (1995)

Ann R. Hunt John T. Roehrig

Enzootic

Togaviridae

Epizootic

Equidae

10.1016/0264-410x(95)93315-z

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Citations (18)

A synthetic peptide to the E glycoprotein of Murray Valley encephalitis virus defines multiple virus-reactive T- and B-cell epitopes

Journal of Virology (1992)

James H. Mathews John T. Roehrig John R. Brubaker Ann R. Hunt Jane E. Allan

Synthetic peptides from the envelope glycoprotein sequence of Murray Valley encephalitis (MVE) virus were previously evaluated in various strains of mice for both the induction of antibody and the in vitro proliferation of peptide-primed T-helper (Th) cells. MVE peptide 6 (amino acids 230 to 251) elicited reciprocal Th- and B-cell reactivity with native MVE virus after primary inoculation of C57BL/6 mice. In this study, we prepared overlapping subunit peptides of MVE peptide 6 and evaluated their immunogenicity. Analysis of these peptides delineated at least two B-cell epitopes that induced antibody reactive with MVE and other Japanese encephalitis serocomplex viruses. This antibody at low titer neutralized MVE virus. Genetic restriction of the antibody response to various T-cell elements within peptide 6 was observed in C3H, BALB/c, C57BL/6, and B10 congenic mice. One element demonstrable after primary immunization, located in the carboxy terminus, associated only with major histocompatibility complex class II IAb and IAbiEk glycoproteins. Functional stimulation with the peptides in association with IAkIEk and IAdIEd molecules was observed only after in vivo secondary stimulation. Peptide 6-1 (amino acids 230 to 241) was nonimmunogenic but could be recognized by Th cells from peptide 6-immunized mice. Further association of peptide 6 with the IAkIEk and IAdIEd subregions was demonstrated by the finding that T cells from MVE peptide 6-inoculated C3H and BALB/c mice primed for an antibody response to MVE virus. These results suggest that the peptide 6 sequence, which is relatively conserved among a number of flaviviruses, should be given consideration when synthetic immunogens for vaccine purposes are designed.

Peptide vaccine

10.1128/jvi.66.11.6555-6562.1992

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Citations (19)

Use of a new synthetic-peptide-derived monoclonal antibody to differentiate between vaccine and wild-type Venezuelan equine encephalomyelitis viruses

Journal of Clinical Microbiology (1991)

John T. Roehrig Richard A. Bolin Ann R. Hunt T M Woodward

We have prepared a murine monoclonal antibody (MAb) capable of distinguishing between wild-type Venezuelan equine encephalomyelitis (VEE) virus and the TC-83 vaccine derivative. This MAb, 1A2B-10, was derived from immunization with a synthetic peptide corresponding to the first 19 amino acids of the E2 glycoprotein of Trinidad donkey VEE virus. The MAb reacts with prototype viruses from all naturally occurring VEE subtypes except subtype 6 in an enzyme-linked immunosorbent assay. It does not react with TC-83 virus or members of the western and eastern equine encephalitis virus complex or with Semliki Forest virus. This antibody will also differentiate between TC-83 and Trinidad donkey VEE virus in indirect immunofluorescence assays with virus-infected Vero cells.

Togaviridae

Vero cell

Semliki Forest virus

10.1128/jcm.29.3.630-631.1991

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Citations (19)