期刊
VIRUSES-BASEL
卷 8, 期 5, 页码 -出版社
MDPI
DOI: 10.3390/v8050149
关键词
Rift Valley fever virus; N-glycosylation; Gn; Gc; sequon; DC-SIGN; L-SIGN
类别
资金
- National Institute of Health [R01 AI087643-01A1]
- James W. McLaughlin predoctoral fellowship
- Sealy Center for Vaccine Development at the UTMB
- Training in Emerging Infectious Diseases and Biodefense grant from the National Institute of Health [T32 AI007536]
- James W. McLaughlin Fellowship Fund at the UTMB
Rift Valley fever is a mosquito-transmitted, zoonotic disease that infects humans and ruminants. Dendritic cell specific intercellular adhesion molecule 3 (ICAM-3) grabbing non-integrin (DC-SIGN) acts as a receptor for members of the phlebovirus genus. The Rift Valley fever virus (RVFV) glycoproteins (Gn/Gc) encode five putative N-glycan sequons (asparagine (N)-any amino acid (X)-serine (S)/threonine (T)) at positions: N438 (Gn), and N794, N829, N1035, and N1077 (Gc). The N-glycosylation profile and significance in viral infection via DC-SIGN have not been elucidated. Gc N-glycosylation was first evaluated by using Gc asparagine (N) to glutamine (Q) mutants. Subsequently, we generated a series of recombinant RVFV MP-12 strain mutants, which encode N-to-Q mutations, and the infectivity of each mutant in Jurkat cells stably expressing DC-SIGN was evaluated. Results showed that Gc N794, N1035, and N1077 were N-glycosylated but N829 was not. Gc N1077 was heterogeneously N-glycosylated. RVFV Gc made two distinct N-glycoforms: Gc-large and Gc-small, and N1077 was responsible for Gc-large band. RVFV showed increased infection of cells expressing DC-SIGN compared to cells lacking DC-SIGN. Infection via DC-SIGN was increased in the presence of either Gn N438 or Gc N1077. Our study showed that N-glycans on the Gc and Gn surface glycoproteins redundantly support RVFV infection via DC-SIGN.
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