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Journal of Virology, October 2002, p. 9844-9855, Vol. 76, No. 19
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.19.9844-9855.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of Three Immunodominant Structural Proteins of Fowlpox Virus

Denise Boulanger,1,{dagger} Philip Green,1 Brenda Jones,1 Gwenn Henriquet,1 Lawrence G. Hunt,1 Stephen M. Laidlaw,1 Paul Monaghan,2 and Michael A. Skinner1*

Compton Laboratory, Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN,1 Pirbright Laboratory, Institute for Animal Health, Pirbright, Woking, Surrey GU24 0NF, United Kingdom2

Received 22 April 2002/ Accepted 19 June 2002

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.


* Corresponding author. Mailing address: Institute for Animal Health, Compton, Newbury, Berkshire RG20 7NN, United Kingdom. Phone: (44) 1635-577270. Fax: (44) 1635-577263. E-mail: michael.skinner{at}bbsrc.ac.uk.

{dagger} Present address: Cancer Sciences Division, University of Southampton School of Medicine, Southampton General Hospital, Southampton SO16 6YD, United Kingdom.


Journal of Virology, October 2002, p. 9844-9855, Vol. 76, No. 19
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.19.9844-9855.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




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Copyright © 2002 by the American Society for Microbiology. All rights reserved.