PMID- 23035215
OWN - NLM
STAT- MEDLINE
DCOM- 20130128
LR  - 20211021
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 86
IP  - 24
DP  - 2012 Dec
TI  - Recognition of the different structural forms of the capsid protein determines 
      the outcome following infection with porcine circovirus type 2.
PG  - 13508-14
LID - 10.1128/JVI.01763-12 [doi]
AB  - Porcine circovirus type 2 (PCV2) capsid protein (CP) is the only protein 
      necessary for the formation of the virion capsid, and recombinant CP 
      spontaneously forms virus-like particles (VLPs). Located within a single CP 
      subunit is an immunodominant epitope consisting of residues 169 to 180 
      [CP(169-180)], which is exposed on the surface of the subunit, but, in the 
      structural context of the VLP, the epitope is buried and inaccessible to 
      antibody. High levels of anti-CP(169-180) activity are associated with porcine 
      circovirus-associated disease (PCVAD). The purpose of this study was to 
      investigate the role of the immune response to monomer CP in the development of 
      PCVAD. The approach was to immunize pigs with CP monomer, followed by challenge 
      with PCV2 and porcine reproductive and respiratory syndrome virus (PRRSV). To 
      maintain the CP immunogen as a stable monomer, CP(43-233) was fused to ubiquitin 
      (Ub-CP). Size exclusion chromatography showed that Ub-CP was present as a single 
      33-kDa protein. Pigs immunized with Ub-CP developed a strong antibody response to 
      PCV2, including antibodies against CP(169-180). However, only low levels of virus 
      neutralizing activity were detected, and viremia levels were similar to those of 
      nonimmunized pigs. As a positive control, immunization with baculovirus-expressed 
      CP (Bac-CP) resulted in high levels of virus neutralizing activity, small amounts 
      of anti-CP(169-180) activity, and the absence of viremia in pigs following virus 
      challenge. The data support the role of CP(169-180) as an immunological decoy and 
      illustrate the importance of the structural form of the CP immunogen in 
      determining the outcome following infection.
FAU - Trible, Benjamin R
AU  - Trible BR
AD  - Department of Diagnostic Medicine and Pathobiology, Kansas State University, 
      Manhattan, Kansas, USA.
FAU - Suddith, Andrew W
AU  - Suddith AW
FAU - Kerrigan, Maureen A
AU  - Kerrigan MA
FAU - Cino-Ozuna, Ada G
AU  - Cino-Ozuna AG
FAU - Hesse, Richard A
AU  - Hesse RA
FAU - Rowland, Raymond R R
AU  - Rowland RR
LA  - eng
GR  - P41 RR001081/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20121003
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Antibodies, Viral)
RN  - 0 (Capsid Proteins)
RN  - 0 (DNA Primers)
SB  - IM
MH  - Antibodies, Viral/immunology
MH  - Base Sequence
MH  - Capsid Proteins/*metabolism
MH  - Chromatography, Gel
MH  - Circoviridae Infections/metabolism/*physiopathology
MH  - Circovirus/immunology/*metabolism
MH  - DNA Primers
MH  - Immunohistochemistry
MH  - Neutralization Tests
PMC - PMC3503079
EDAT- 2012/10/05 06:00
MHDA- 2013/01/29 06:00
PMCR- 2013/06/01
CRDT- 2012/10/05 06:00
PHST- 2012/10/05 06:00 [entrez]
PHST- 2012/10/05 06:00 [pubmed]
PHST- 2013/01/29 06:00 [medline]
PHST- 2013/06/01 00:00 [pmc-release]
AID - JVI.01763-12 [pii]
AID - 01763-12 [pii]
AID - 10.1128/JVI.01763-12 [doi]
PST - ppublish
SO  - J Virol. 2012 Dec;86(24):13508-14. doi: 10.1128/JVI.01763-12. Epub 2012 Oct 3.