Deletion of N-glycosylation sites of hepatitis C virus envelope protein E1 enhances specific cellular and humoral immune responses

Liu, Min; Chen, Haidan; Luo, Fang; Li, Pingfei; Pan, Qin; Xia, Bing; Qi, Zhongtian; Ho, Wen‐Zhe; Zhang, Xiaolian

doi:10.1016/j.vaccine.2007.07.003

Cited by 41 publications

(48 citation statements)

References 23 publications

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“…As previously observed for viruses such as simian immunodeficiency virus (38), human immunodeficiency virus (45), influenza virus (44), hepatitis C virus (24), and Ebola virus (16), PRRSV also relies on glycosylation modification of its envelope proteins to evade the host immune response (3,15). Our laboratory has previously demonstrated that removal of N-glycosylation sites surrounding the neutralizing epitope located in GP5 of a PRRSV strain (FL12) renders the virus extremely susceptible to antibody neutralization (3).…”

mentioning

confidence: 74%

Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3

Kwon

Yoon

et al. 2011

J Virol

107

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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.

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confidence: 74%

Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3

Kwon

Yoon

et al. 2011

J Virol

107

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“…Site-directed mutagenic studies on other single-stranded positivesense RNA viruses revealed that the deletion of N-glycosylation sites enhance the host immune response and decrease the virulence (e.g. Liu et al, 2007;Sainz et al, 2008). Drugs that inhibit viral N-glycosylation of the virus envelope are currently being tested for preventing viral infection (e.g.…”

Section: Resultsmentioning

confidence: 99%

Detection of positive selection in the major capsid protein VP60 of the rabbit haemorrhagic disease virus (RHDV)

et al. 2008

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a b s t r a c tMutations were analysed in the major capsid protein VP60 of the rabbit haemorrhagic disease virus (RHDV), a calicivirus responsible for high mortality rates in both wild and domestic European rabbits (Oryctolagus cuniculus). Likelihood of positive selection was estimated using the PAML software applied to 43 non-identical complete sequences of the major capsid protein. Three codons showed signs of positive selection (with posterior probabilities over 95%), one of them is located in the region containing the major antigenic determinants (region E). The presence of positively selected codons (PSCs) in other regions may suggest the existence of other antigenic regions on the major capsid protein that stimulate protective immune responses. At all the 3 PSCs, variation contributes to putative N-glycosylation sites of the protein.An N-glycosylation site is deleted in the non-pathogenic strain RCV. Some of the substitutions at PSCs may alter the polarity and the charge of the protein with possible implications in the protein structure and host interaction. The detection of PSCs should allow a better understanding of the interaction between RHDV and the rabbit immune system.

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“…Bacteria CFU (colony forming units) were quantified from the absorbance at 600 nm. The anti-E1 or anti-E2 polyclonal antibodies were prepared as our previous publications (29,30).…”

Section: Cell Lines Bacteria and Reagentsmentioning

confidence: 99%

“…The cell lysates samples were electrophoresed in 12 % SDS-polyacrylamide gels under reducing conditions. After transfer from the gels to polyvinylidene difluoride membranes (Millipore), the proteins were probed with anti-L-ficolin, anti-E1 or anti-E2 polyclonal antibodies (29,30), and then incubated with HRP conjugated anti-rabbit IgG (1:2000 dilution). Color was developed with Nitroblue-tetrazolium and Bromo-chloroindolyl-phosphate.…”

Section: Sds-page and Western Blot Analysismentioning

confidence: 99%

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Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation

Liu

Ali

et al. 2009

Cell Mol Immunol

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L-ficolin, one of lectin families, is a recently identified complement factor that initiates lectin pathway of complement. Little is known about its role in viral hepatitis. In the present study, we found that L-ficolin in serum from 103 patients with hepatitis C virus (HCV), were significantly higher than that in 150 healthy controls. We further found that L-ficolin expressions were significantly increased in vitro study by HCV JFH-1 infected human hepatocyte cell line Huh7.5.

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Deletion of N-glycosylation sites of hepatitis C virus envelope protein E1 enhances specific cellular and humoral immune responses

Cited by 41 publications

References 23 publications

Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3

Immune Evasion of Porcine Reproductive and Respiratory Syndrome Virus through Glycan Shielding Involves both Glycoprotein 5 as Well as Glycoprotein 3

Detection of positive selection in the major capsid protein VP60 of the rabbit haemorrhagic disease virus (RHDV)

Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation

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