Mapping epitopes in equine rhinitis A virus VP1 recognized by antibodies elicited in response to infection of the natural host.
Equine rhinitis A virus (ERAV) is an important respiratory pathogen of horses and is of additional interest because of its close relationship and common classification with foot-and-mouth disease virus (FMDV). As is the case with FMDV, the VP1 capsid protein of ERAV has been shown to be a target of neutralizing antibodies. In FMDV VP1, such antibodies commonly recognize linear epitopes present in the betaG-betaH loop region. To map linear B cell epitopes in ERAV VP1, overlapping fragments spanning its length were expressed in Escherichia coli as glutathione S-transferase (GST) fusion proteins. These fusion proteins were tested for reactivity with sera from ERAV-infected horses and with polyclonal sera from ERAV-immunized rabbits and mice. Regions at the N- and C-termini as well as the betaE-betaF and the betaG-betaH loop regions contained B cell epitopes that elicited antibodies in the natural host. GST fusion proteins of these regions also elicited antibodies following immunization of rabbits and mice, which, in general, strongly recognized native ERAV VP1 but which were non-neutralizing. It is concluded that the N-terminal region of ERAV VP1, in particular, contains strong B cell epitopes.
Stevenson
Rachel A
RA
Centre for Equine Virology, School of Veterinary Science, The University of Melbourne, Victoria 3010, Australia.
Hartley
Carol A
CA
Centre for Equine Virology, School of Veterinary Science, The University of Melbourne, Victoria 3010, Australia.
Huang
Jin-An
JA
Centre for Equine Virology, School of Veterinary Science, The University of Melbourne, Victoria 3010, Australia.
Studdert
Michael J
MJ
Centre for Equine Virology, School of Veterinary Science, The University of Melbourne, Victoria 3010, Australia.
Crabb
Brendan S
BS
The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3050, Australia.
Warner
Simone
S
Department of Microbiology and Immunology and the Co-operative Research Centre for Vaccine Technology, The University of Melbourne, Victoria 3010, Australia.
D000595:Amino Acid Sequence; D000818:Animals; D000914:Antibodies, Viral; D000956:Antigens, Viral / Q000235:genetics; D005537:Aphthovirus / Q000235:genetics / Q000276:immunology* / Q000472:pathogenicity; D036022:Capsid Proteins / Q000235:genetics / Q000276:immunology*; D018604:Epitope Mapping; D006734:Horse Diseases / Q000276:immunology / Q000821:virology; D006736:Horses; D008969:Molecular Sequence Data; D010850:Picornaviridae Infections / Q000276:immunology / Q000662:veterinary / Q000821:virology; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology
D000914:Antibodies, Viral; D000956:Antigens, Viral; D036022:Capsid Proteins; D011993:Recombinant Fusion Proteins