PMID- 22761373
OWN - NLM
STAT- MEDLINE
DCOM- 20121121
LR  - 20211021
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 86
IP  - 18
DP  - 2012 Sep
TI  - N-linked glycosylation of GP5 of porcine reproductive and respiratory syndrome 
      virus is critically important for virus replication in vivo.
PG  - 9941-51
LID - 10.1128/JVI.07067-11 [doi]
AB  - It has been proposed that the N-linked glycan addition at certain sites in GP5 of 
      porcine reproductive and respiratory syndrome virus (PRRSV) is important for 
      production of infectious viruses and viral infectivity. However, such specific 
      N-linked glycosylation sites do not exist in some field PRRSV isolates. This 
      implies that the existence of GP5-associated glycan per se is not vital to the 
      virus life cycle. In this study, we found that mutation of individual 
      glycosylation sites at N30, N35, N44, and N51 in GP5 did not affect virus 
      infectivity in cultured cells. However, the mutants carrying multiple mutations 
      at N-linked glycosylation sites in GP5 had significantly reduced virus yields 
      compared with the wild-type (wt) virus. As a result, no viremia and antibody 
      response were detected in piglets that were injected with a mutant without all 
      N-linked glycans in GP5. These results suggest that the N-linked glycosylation of 
      GP5 is critically important for virus replication in vivo. The study also showed 
      that removal of N44-linked glycan from GP5 increased the sensitivity of mutant 
      virus to convalescent-phase serum samples but did not elicit a high-level 
      neutralizing antibody response to wt PRRSV. The results obtained from the present 
      study have made significant contributions to better understanding the importance 
      of glycosylation of GP5 in the biology of PRRSV.
FAU - Wei, Zuzhang
AU  - Wei Z
AD  - Department of Swine Infectious Diseases, Shanghai Veterinary Research Institute, 
      Chinese Academy of Agricultural Sciences, Shanghai, China.
FAU - Lin, Tao
AU  - Lin T
FAU - Sun, Lichang
AU  - Sun L
FAU - Li, Yanhua
AU  - Li Y
FAU - Wang, Xiaoming
AU  - Wang X
FAU - Gao, Fei
AU  - Gao F
FAU - Liu, Runxia
AU  - Liu R
FAU - Chen, Chunyan
AU  - Chen C
FAU - Tong, Guangzhi
AU  - Tong G
FAU - Yuan, Shishan
AU  - Yuan S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120703
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Antibodies, Neutralizing)
RN  - 0 (Antibodies, Viral)
RN  - 0 (DNA, Viral)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (glycoprotein 5, PRRSV)
SB  - IM
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Animals
MH  - Antibodies, Neutralizing/blood
MH  - Antibodies, Viral/blood
MH  - Base Sequence
MH  - Binding Sites/genetics
MH  - Cell Line
MH  - DNA, Viral/genetics
MH  - Glycosylation
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Porcine Reproductive and Respiratory Syndrome/immunology/virology
MH  - Porcine respiratory and reproductive syndrome 
      virus/genetics/immunology/*physiology
MH  - Swine
MH  - Viral Envelope Proteins/*chemistry/genetics/immunology/*physiology
MH  - Virus Replication/genetics/physiology
PMC - PMC3446624
EDAT- 2012/07/05 06:00
MHDA- 2012/12/10 06:00
PMCR- 2013/03/01
CRDT- 2012/07/05 06:00
PHST- 2012/07/05 06:00 [entrez]
PHST- 2012/07/05 06:00 [pubmed]
PHST- 2012/12/10 06:00 [medline]
PHST- 2013/03/01 00:00 [pmc-release]
AID - JVI.07067-11 [pii]
AID - 07067-11 [pii]
AID - 10.1128/JVI.07067-11 [doi]
PST - ppublish
SO  - J Virol. 2012 Sep;86(18):9941-51. doi: 10.1128/JVI.07067-11. Epub 2012 Jul 3.