2005
DOI: 10.1016/j.vaccine.2004.11.068
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Role of the N-linked glycans of the prM and E envelope proteins in tick-borne encephalitis virus particle secretion

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Cited by 61 publications
(62 citation statements)
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“…We previously examined the role of the N-linked glycans of E protein in tick-borne encephalitis-virus particle secretion using subviral particles. 13 Secretion of virus particles was greatly reduced in culture cells transfected with mutant vectors that have an amino acid substitution of T156A in the E protein, and the study also suggested that the reduced particle secretion is caused by glycan loss rather than to the amino acid substitution per se. The amino acid substitution of T156A is similar to that of S156P in our current study in terms of amino acid characteristics, and both mutations altered the protein such that it would not be recognized by oligosaccharyl-transferase.…”
Section: Discussionmentioning
confidence: 93%
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“…We previously examined the role of the N-linked glycans of E protein in tick-borne encephalitis-virus particle secretion using subviral particles. 13 Secretion of virus particles was greatly reduced in culture cells transfected with mutant vectors that have an amino acid substitution of T156A in the E protein, and the study also suggested that the reduced particle secretion is caused by glycan loss rather than to the amino acid substitution per se. The amino acid substitution of T156A is similar to that of S156P in our current study in terms of amino acid characteristics, and both mutations altered the protein such that it would not be recognized by oligosaccharyl-transferase.…”
Section: Discussionmentioning
confidence: 93%
“…23 -25 But there was no report studying the relationship among temperature sensitivity of WN virus, the glycosylation of envelope protein, and the intracellular viral protein maturation and trafficking. Our previous study 13 using a subviral system of tick-borne encephalitis virus showed that a mutant lacking E-protein glycosylation has a large reduction in the level of secretion of the E protein; the E protein is retained at the endoplasmic reticulum and is rarely present in the Golgi complex. In the dengue virus, this glycosylation at aa154 occurs in E-protein domain I, close to the center of the fusion peptide of E-protein domain II, and glycosylation of the E protein is considered to increase the stability of the protein.…”
Section: Discussionmentioning
confidence: 99%
“…Although glycosylation of flavivirus premembrane proteins appears to be absolutely required for efficient virion assembly and maturation, 16,[25][26][27][28] WNV strains lacking a glycosylation site in the E protein have been isolated from naturally infected vertebrates and mosquitoes. [8][9][10][11][12][13] Previously, we have shown that WNV lacking the E protein glycan is attenuated in the natural vector species Cx.…”
Section: Discussionmentioning
confidence: 99%
“…In one study, the correlation between the presence of such sites and antigenic properties of flavivirus was not established because deglycosylated viruses could maintain the same antigenicity (Winkler et al, 1987). On the other hand, in other more recent studies, glycosylation was found to be very important for viral replication, virulence, maturation or release of viral-like particles (Beasley et al, 2005;Crabtree et al, 2005;Goto et al, 2005;Li et al, 2006).…”
Section: Discussionmentioning
confidence: 99%
“…In one study, the correlation between the presence of such sites and antigenic properties of flavivirus was not established because deglycosylated viruses could maintain the same antigenicity (Winkler et al, 1987). On the other hand, in other more recent studies, glycosylation was found to be very important for viral replication, virulence, maturation or release of viral-like particles (Beasley et al, 2005;Crabtree et al, 2005;Goto et al, 2005;Li et al, 2006).Our analysis of the conserved motifs showed that ROCV shares numerous conserved amino acid and/or peptides with several flaviviruses across different groups, each with a varied host range. Interestingly, in the E protein, the tripeptide (TGP) of ROCV within domain III was found to be different from those observed in all other JEV members (RGX, where X is D, E or T).…”
mentioning
confidence: 99%