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Identification and Characterization of Three Immunodominant Structural Proteins of Fowlpox Virus

Identification and Characterization of Three Immunodominant Structural Proteins of Fowlpox Virus
Identification and Characterization of Three Immunodominant Structural Proteins of Fowlpox Virus
Genes encoding fowlpox virus (FWPV) structural proteins have been identified mainly by sequence homology with those from vaccinia virus (VACV), but little is known about the encoded proteins. Production of monoclonal antibodies (MAbs) against Poxine and HP1-440 (Munich) clone FP9 allowed the identification of three immunodominant FWPV proteins: the 39-kDa core protein (encoded by FPV168, homologous to VACV A4L), a 30- and 35-kDa protein doublet, and an abundant 63-kDa protein. The 30- and 35-kDa proteins are nonglycosylated, antigenically related proteins present in the intracellular mature virus membrane and localizing closely with the viral factories. N-terminal sequencing identified the 35-kDa protein as encoded by FPV140 (the FWPV homolog of VACV H3L). The 63-kDa protein forms covalently linked dimers and oligomers. It remained mainly insoluble upon detergent treatment of purified virus but did not localize closely with the viral factory. N-terminal sequencing was unsuccessful, suggesting N-terminal blocking. CNBr digestion generated a peptide encoded by FPV191, predicted to encode one of two FWPV A-type inclusion (ATI) proteins. The characteristics of the 63-kDa protein were inconsistent with published observations on cowpox or VACV ATI proteins (it appears to be essential). The 63-kDa protein, however, shares characteristics with both VACV p4c virus occlusion and 14-kDa fusion proteins. Gene assignment at the poxvirus ATI locus (between VACV A24R and A28L) is complicated by sequence redundancies and variations, often due to deletions and multiple frameshift mutations. The identity of FPV191 in relation to genes at this locus is discussed.
0022-538X
9844-9855
Boulanger, Denise
c226ad99-9c9a-485a-b480-42fb8799120f
Green, Philip
7d21c5c7-6be1-4174-a48f-08867663f8e7
Jones, Brenda
11c85783-d04b-42c8-bf92-a7b65cd1329e
Henriquet, Gwenn
95d3c534-b3ef-4eca-8906-2e02930ed0cf
Hunt, Lawrence G.
c61092e6-cb33-48f4-bfcc-08227d385bad
Laidlaw, Stephen M.
72fcf066-0e44-4d02-9b65-f76d4251bfcf
Monaghan, Paul
9458fbf6-908c-475b-ba8f-2a435af813d9
Skinner, Michael A.
dd116d23-f3e6-40b2-a7e0-b0ea10cacc40
Boulanger, Denise
c226ad99-9c9a-485a-b480-42fb8799120f
Green, Philip
7d21c5c7-6be1-4174-a48f-08867663f8e7
Jones, Brenda
11c85783-d04b-42c8-bf92-a7b65cd1329e
Henriquet, Gwenn
95d3c534-b3ef-4eca-8906-2e02930ed0cf
Hunt, Lawrence G.
c61092e6-cb33-48f4-bfcc-08227d385bad
Laidlaw, Stephen M.
72fcf066-0e44-4d02-9b65-f76d4251bfcf
Monaghan, Paul
9458fbf6-908c-475b-ba8f-2a435af813d9
Skinner, Michael A.
dd116d23-f3e6-40b2-a7e0-b0ea10cacc40

Boulanger, Denise, Green, Philip, Jones, Brenda, Henriquet, Gwenn, Hunt, Lawrence G., Laidlaw, Stephen M., Monaghan, Paul and Skinner, Michael A. (2002) Identification and Characterization of Three Immunodominant Structural Proteins of Fowlpox Virus. Journal of Virology, 76 (19), 9844-9855. (doi:10.1128/jvi.76.19.9844-9855.2002).

Record type: Article

Abstract

Genes encoding fowlpox virus (FWPV) structural proteins have been identified mainly by sequence homology with those from vaccinia virus (VACV), but little is known about the encoded proteins. Production of monoclonal antibodies (MAbs) against Poxine and HP1-440 (Munich) clone FP9 allowed the identification of three immunodominant FWPV proteins: the 39-kDa core protein (encoded by FPV168, homologous to VACV A4L), a 30- and 35-kDa protein doublet, and an abundant 63-kDa protein. The 30- and 35-kDa proteins are nonglycosylated, antigenically related proteins present in the intracellular mature virus membrane and localizing closely with the viral factories. N-terminal sequencing identified the 35-kDa protein as encoded by FPV140 (the FWPV homolog of VACV H3L). The 63-kDa protein forms covalently linked dimers and oligomers. It remained mainly insoluble upon detergent treatment of purified virus but did not localize closely with the viral factory. N-terminal sequencing was unsuccessful, suggesting N-terminal blocking. CNBr digestion generated a peptide encoded by FPV191, predicted to encode one of two FWPV A-type inclusion (ATI) proteins. The characteristics of the 63-kDa protein were inconsistent with published observations on cowpox or VACV ATI proteins (it appears to be essential). The 63-kDa protein, however, shares characteristics with both VACV p4c virus occlusion and 14-kDa fusion proteins. Gene assignment at the poxvirus ATI locus (between VACV A24R and A28L) is complicated by sequence redundancies and variations, often due to deletions and multiple frameshift mutations. The identity of FPV191 in relation to genes at this locus is discussed.

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Published date: 1 October 2002
Additional Information: Copyright © 2002 American Society for Microbiology

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Local EPrints ID: 458112
URI: http://eprints.soton.ac.uk/id/eprint/458112
ISSN: 0022-538X
PURE UUID: b584e855-7ebd-478c-8693-4cf4f5cd46e8
ORCID for Denise Boulanger: ORCID iD orcid.org/0000-0003-1000-7313

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Date deposited: 28 Jun 2022 17:07
Last modified: 17 Mar 2024 02:57

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Author: Denise Boulanger ORCID iD
Author: Philip Green
Author: Brenda Jones
Author: Gwenn Henriquet
Author: Lawrence G. Hunt
Author: Stephen M. Laidlaw
Author: Paul Monaghan
Author: Michael A. Skinner

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