Langat virus M protein is structurally homologous to prM

M. R. Holbrook; H. Wang; A. D.T. Barrett

doi:10.1128/JVI.75.8.3999-4001.2001

Langat virus M protein is structurally homologous to prM

M. R. Holbrook, H. Wang, A. D.T. Barrett

Pathology

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Langat (LGT) virus M protein has been generated in a recombinant system. Antiserum raised against the LGT virus M protein neutralizes tick-borne encephalitis serocomplex flaviviruses but not mosquito-borne flaviviruses, indicating that the M protein is exposed on the surface of virions. The antiserum recognizes intracellular LGT virus prM/M and binds to prM and M in Western blots of whole-cell lysates and purified virus, respectively. These data suggest that the prM and M proteins are structurally similar under native conditions and support the hypothesis that the "pr" portion of prM facilitates proper folding of the M protein for expression on the virion surface.

Original language	English (US)
Pages (from-to)	3999-4001
Number of pages	3
Journal	Journal of virology
Volume	75
Issue number	8
DOIs	https://doi.org/10.1128/JVI.75.8.3999-4001.2001
State	Published - 2001

ASJC Scopus subject areas

Microbiology
Immunology
Insect Science
Virology

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10.1128/JVI.75.8.3999-4001.2001

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title = "Langat virus M protein is structurally homologous to prM",

abstract = "Langat (LGT) virus M protein has been generated in a recombinant system. Antiserum raised against the LGT virus M protein neutralizes tick-borne encephalitis serocomplex flaviviruses but not mosquito-borne flaviviruses, indicating that the M protein is exposed on the surface of virions. The antiserum recognizes intracellular LGT virus prM/M and binds to prM and M in Western blots of whole-cell lysates and purified virus, respectively. These data suggest that the prM and M proteins are structurally similar under native conditions and support the hypothesis that the {"}pr{"} portion of prM facilitates proper folding of the M protein for expression on the virion surface.",

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AU - Holbrook, M. R.

AU - Wang, H.

AU - Barrett, A. D.T.

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AB - Langat (LGT) virus M protein has been generated in a recombinant system. Antiserum raised against the LGT virus M protein neutralizes tick-borne encephalitis serocomplex flaviviruses but not mosquito-borne flaviviruses, indicating that the M protein is exposed on the surface of virions. The antiserum recognizes intracellular LGT virus prM/M and binds to prM and M in Western blots of whole-cell lysates and purified virus, respectively. These data suggest that the prM and M proteins are structurally similar under native conditions and support the hypothesis that the "pr" portion of prM facilitates proper folding of the M protein for expression on the virion surface.

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Langat virus M protein is structurally homologous to prM

Abstract

ASJC Scopus subject areas

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