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Liang L.,U.S. Center for Disease Control and Prevention | Liang L.,Sun Yat Sen University | Huang P.,U.S. Center for Disease Control and Prevention | Huang P.,Sun Yat Sen University | And 5 more authors.
Acta Biochimica et Biophysica Sinica | Year: 2012

The virus surface protein neuraminidase (NA) is a main subtype-specific antigen in influenza type A viruses. Neuraminidase functions as an enzyme to break the bonds between hemagglutinin (HA) and sialic acid to release newly formed viruses from infected cells. In this study, NA genes from the H3N2 subtype virus were sequenced and NA proteins were screened for B-cell epitopes and assessed based on immunoinformatics. Based on this information, three peptides ES8, RR9, and WK7 (covering amino acid residues 221-228, 292-300, and 383-389, respectively) of the NA protein were selected and synthesized artificially. These peptides were used to immunize New Zealand rabbits subcutaneously to raise antisera. Results showed that these three peptides were capable of eliciting antibodies against H3N2 viruses in a specific and sensitive manner, detected in vitro by enzyme-linked immunosorbent assay. Furthermore, hemadsorption anti-releasing effects occurred in three antisera mixtures at a dilution of 1:40. Alignment using database software showed that amino acid residues in these three epitope peptides were substituted at specific sites in all the NAs sequenced in this study. We suggest that these NA epitope peptides might be used in conjunction with HA proteins as vaccine antigens. © The Author 2011.


Huang P.,U.S. Center for Disease Control and Prevention | Xu Y.-S.,Sinoasis Pharmaceuticals Guangzhou Inc. | Zhong J.,Guangzhou Chest Hospital | Ni H.-Z.,U.S. Center for Disease Control and Prevention | And 4 more authors.
Progress in Biochemistry and Biophysics | Year: 2011

The neuraminidase (NA) of influenza virus is a receptor-destroying enzyme, removing sialic acid from carbohydrate chains attached to HA, and releasing the viruses from infected cells. The NA genes of the 2009 A H1N1 were sequenced, then the B-cell epitopes were predicted, screened and assessed based on immunoinformatics. Two peptides SE8 and RE6 (amino acid residues 168̃175 and 428̃433) of NA protein were synthesized and immunized to raise antisera in rabbits. Two antisera are capable of eliciting neutralizing antibodies against 2009A H1N1 in the in vitro microneutralization assay, furthermore, the anti-releasing effects of hemagglutination existed in the antisera. Alignment with databases showed that the amino acid residues of two epitope peptides are highly conserved amongst the NA sequences of the strains isolated fromthe world. These findings indicate that SE8 and RE6 represents an attractive candidate for an effective synthetic peptide-based vaccine against 2009 A H1N1 viruses.


Huang P.,U.S. Center for Disease Control and Prevention | Xu Y.,Sinoasis Pharmaceuticals Guangzhou Inc. | Ni H.,U.S. Center for Disease Control and Prevention | Zhong J.,Guangzhou Chest Hospital | And 8 more authors.
Vaccine | Year: 2011

The 2009 A H1N1 viruses have spread throughout the world, as the viral neuraminidase (NA) is a receptor-destroying enzyme, removing sialic acid from carbohydrate chains attached to NA, and releasing the viruses from infected cells. In this study, the NA genes of Guangdong viruses were sequenced, then their B-cell epitopes were predicted, screened and assessed based on immunoinformatics. The antisera were raised in rabbits against five linear synthetic peptides spanning the NA protein of 2009 A H1N1. Five peptides, LR17, SS12, DP9, DS11 and DI14, respectively, are capable of eliciting neutralizing antibodies against 2009 A H1N1 in the in vitro microneutralization assay. DI14 was identified to be particularly potent in eliciting a neutralizing antibody titer comparable to that obtained with a whole virion-immunized serum. Immunization of rabbit with either five peptides triggered a 2009 A H1N1-specific antibody response as high as that obtained with the whole virion as immunogen. Alignment with databases showed that the amino acid residues of five epitope peptides are highly conserved among the NA sequences of 2009 A H1N1 strains isolated from the world. Altogether, these data indicate that LR17, SS12, DP9, DS11 and DI14 represent a promising candidate for an effective synthetic peptide-based vaccine against 2009 A H1N1 viruses. © 2010 Elsevier Ltd.

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