PMID- 21411530
OWN - NLM
STAT- MEDLINE
DCOM- 20110713
LR  - 20211020
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 85
IP  - 11
DP  - 2011 Jun
TI  - Immune evasion of porcine reproductive and respiratory syndrome virus through 
      glycan shielding involves both glycoprotein 5 as well as glycoprotein 3.
PG  - 5555-64
LID - 10.1128/JVI.00189-11 [doi]
AB  - Passive administration of porcine reproductive and respiratory syndrome virus 
      (PRRSV) neutralizing antibodies (NAbs) can effectively protect pigs against PRRSV 
      infection. However, after PRRSV infection, pigs typically develop a weak and 
      deferred NAb response. One major reason for such a meager NAb response is the 
      phenomenon of glycan shielding involving GP5, a major glycoprotein carrying one 
      major neutralizing epitope. We describe here a type II PRRSV field isolate 
      (PRRSV-01) that is highly susceptible to neutralization and induces an atypically 
      rapid, robust NAb response in vivo. Sequence analysis shows that PRRSV-01 lacks 
      two N-glycosylation sites, normally present in wild-type (wt) PRRSV strains, in 
      two of its envelope glycoproteins, one in GP3 (position 131) and the other in GP5 
      (position 51). To determine the influence of these missing N-glycosylation sites 
      on the distinct neutralization phenotype of PRRSV-01, a chimeric virus (FL01) was 
      generated by replacing the structural genes of type II PRRSV strain FL12 cDNA 
      infectious clone with those from PRRSV-01. N-glycosylation sites were 
      reintroduced into GP3 and GP5 of FL01, separately or in combination, by 
      site-directed mutagenesis. Reintroduction of the N-glycosylation site in either 
      GP3 or GP5 allowed recovery of in vivo and in vitro glycan shielding capacity, 
      with an additive effect when these sites were reintroduced into both 
      glycoproteins simultaneously. Although the loss of these glycosylation sites has 
      seemingly occurred naturally (presumably by passage through cell cultures), 
      PRRSV-01 virus quickly regains these glycosylation sites through replication in 
      vivo, suggesting that a strong selective pressure is exerted at these sites. 
      Collectively, our data demonstrate the involvement of an N-glycan moiety located 
      in GP3 in glycan shield interference.
FAU - Vu, Hiep L X
AU  - Vu HL
AD  - Nebraska Center for Virology and School of Veterinary Medicine and Biomedical 
      Sciences, University of Nebraska-Lincoln, Lincoln, NE, USA.
FAU - Kwon, Byungjoon
AU  - Kwon B
FAU - Yoon, Kyoung-Jin
AU  - Yoon KJ
FAU - Laegreid, William W
AU  - Laegreid WW
FAU - Pattnaik, Asit K
AU  - Pattnaik AK
FAU - Osorio, Fernando A
AU  - Osorio FA
LA  - eng
SI  - GENBANK/JF422072
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20110316
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Antibodies, Neutralizing)
RN  - 0 (Antibodies, Viral)
RN  - 0 (Glycoproteins)
RN  - 0 (Polysaccharides)
RN  - 0 (RNA, Viral)
RN  - 0 (Viral Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies, Neutralizing/immunology
MH  - Antibodies, Viral/immunology
MH  - Cell Line
MH  - Glycoproteins/genetics/*immunology
MH  - *Immune Evasion
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Mutation, Missense
MH  - Polysaccharides/*metabolism
MH  - Porcine respiratory and reproductive syndrome virus/*immunology/*pathogenicity
MH  - RNA, Viral/genetics
MH  - Sequence Analysis, DNA
MH  - Swine
MH  - Viral Plaque Assay
MH  - Viral Proteins/genetics/*immunology
PMC - PMC3094951
EDAT- 2011/03/18 06:00
MHDA- 2011/07/14 06:00
PMCR- 2011/12/01
CRDT- 2011/03/18 06:00
PHST- 2011/03/18 06:00 [entrez]
PHST- 2011/03/18 06:00 [pubmed]
PHST- 2011/07/14 06:00 [medline]
PHST- 2011/12/01 00:00 [pmc-release]
AID - JVI.00189-11 [pii]
AID - 0189-11 [pii]
AID - 10.1128/JVI.00189-11 [doi]
PST - ppublish
SO  - J Virol. 2011 Jun;85(11):5555-64. doi: 10.1128/JVI.00189-11. Epub 2011 Mar 16.