PMID- 12029156
OWN - NLM
STAT- MEDLINE
DCOM- 20020711
LR  - 20200218
IS  - 0022-1317 (Print)
IS  - 0022-1317 (Linking)
VI  - 83
IP  - Pt 6
DP  - 2002 Jun
TI  - Porcine B-cells recognize epitopes that are conserved between the structural 
      proteins of American- and European-type porcine reproductive and respiratory 
      syndrome virus.
PG  - 1407-1418
LID - 10.1099/0022-1317-83-6-1407 [doi]
AB  - By selecting phage display libraries with immune sera from experimentally 
      infected pigs, porcine B-cell epitopes in the open reading frame (ORF) 2, 3, 5 
      and 6 proteins of European-type porcine reproductive and respiratory syndrome 
      virus (PRRSV) were identified. The sequences of all the epitopes were well 
      conserved in European-type PRRSV and even between European- and American-type 
      PRRSV. Accordingly, sera from pigs infected with American-type PRRSV 
      cross-reacted with the European-type epitopes. Thus, this study showed, for the 
      first time, the presence of highly conserved epitopes in the matrix protein and 
      envelope glycoproteins of PRRSV. ORF5 and 6 epitopes localized to protein parts 
      that are predicted to be hidden in PRRSV virions. In contrast, ORF2 and 3 
      epitopes localized to putative protein ectodomains. Due to the interesting 
      localization, the sequence surrounding the ORF2 and 3 epitopes was subjected to 
      closer scrutiny. A heptad motif, VSRRIYQ, which is present in a single copy in 
      ORF2 and 3 proteins, was identified; this arrangement is completely conserved in 
      all European-type PRRSV sequences available. The VSRRIYQ repeat motif colocalized 
      closely with one of the ORF2 epitopes and secondary structure modelling showed 
      that this segment of the ORF2 protein could form an amphipathic helix. 
      Intriguingly, a mutation associated with virulence/attenuation of an American 
      vaccine strain of PRRSV also localized to this ORF2 protein segment and affected 
      the hydrophobic face of the predicted amphipathic helix. Further work is needed 
      to determine whether these findings delineate a functional domain in the PRRSV 
      ORF2 protein.
FAU - Oleksiewicz, M B
AU  - Oleksiewicz MB
AD  - The Danish Veterinary Institute for Virus Research, Lindholm, 4771 Kalvehave, 
      Denmark1.
FAU - Botner, A
AU  - Botner A
AD  - The Danish Veterinary Institute for Virus Research, Lindholm, 4771 Kalvehave, 
      Denmark1.
FAU - Normann, P
AU  - Normann P
AD  - The Danish Veterinary Institute for Virus Research, Lindholm, 4771 Kalvehave, 
      Denmark1.
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - England
TA  - J Gen Virol
JT  - The Journal of general virology
JID - 0077340
RN  - 0 (Antigens, Viral)
RN  - 0 (Glycoproteins)
RN  - 0 (Immune Sera)
RN  - 0 (Peptide Library)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (Viral Structural Proteins)
SB  - IM
MH  - Americas
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antigens, Viral/genetics/immunology
MH  - B-Lymphocytes/*immunology
MH  - Conserved Sequence
MH  - Cross Reactions
MH  - Epitope Mapping
MH  - Europe
MH  - Glycoproteins/immunology
MH  - Immune Sera
MH  - Molecular Sequence Data
MH  - Open Reading Frames
MH  - Peptide Library
MH  - Porcine respiratory and reproductive syndrome virus/*genetics/*immunology
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Swine
MH  - Viral Envelope Proteins/immunology
MH  - Viral Structural Proteins/*immunology
EDAT- 2002/05/25 10:00
MHDA- 2002/07/12 10:01
CRDT- 2002/05/25 10:00
PHST- 2002/05/25 10:00 [pubmed]
PHST- 2002/07/12 10:01 [medline]
PHST- 2002/05/25 10:00 [entrez]
AID - 10.1099/0022-1317-83-6-1407 [doi]
PST - ppublish
SO  - J Gen Virol. 2002 Jun;83(Pt 6):1407-1418. doi: 10.1099/0022-1317-83-6-1407.