Molecular characterization of a major outer capsid protein encoded by the Threadfin aquareovirus (TFV) gene segment 10 (S10).

Autor: Seng EK; Department of Biological Sciences, National University of Singapore, Singapore. dbssek@nus.edu.sg, Fang Q, Sin YM, Lam TJ
Jazyk: angličtina
Zdroj: Archives of virology [Arch Virol] 2005 Oct; Vol. 150 (10), pp. 2021-36. Date of Electronic Publication: 2005 Jun 03.
DOI: 10.1007/s00705-005-0550-9
Abstrakt: Genome segment 10 (S10) of Threadfin aquareovirus (TFV) was cloned, sequenced, analyzed and found to be 987 bp long encoding a protein of 298 aa with a predicted molecular mass of 32.0 kDa. The TFV S10 gene possesses terminal motifs, (5' GTTTTA and ATTCATC 3') which are also conserved in the S6 and S11 TFV gene segments. Sequence comparison revealed that the TFV S10 gene was similar to the Striped bass reovirus (SBR) VP7 outer capsid protein (OCP). A conserved putative zinc-finger motif, CCHC, present in the mammalian reovirus (MRV) delta3 protein, was identified in TFV and other aquareovirus VP7 protein. Phylogenetic analysis of the TFV VP7 protein indicated that TFV is closely related to SBR and Chum salmon reovirus (CSV) and possibly belong to the same species Aquareovirus A as SBR and CSV. The TFV VP7 protein was expressed in E. coli, purified and injected into mice. Serum specific antibodies were generated, however, the serum showed weak neutralizing activity. In contrast, co-incubation of this serum with another serum obtained from mice immunized with another OCP encoded by the TFV S6 gene segment resulted in a highly elevated antibody neutralization titer.
Databáze: MEDLINE