Binding characterization of determinants in porcine aminopeptidase N, the cellular receptor for transmissible gastroenteritis virus.

Journal of Biotechnology
Xiaofeng RenBoqi Liu

Abstract

Four truncated porcine aminopeptidase N (pAPN, a cellular receptor for porcine coronaviruses) proteins were expressed in prokaryotic cells. The recognizing of a specific serum against pAPN to these proteins was investigated by enzyme-linked immunosorbent assay (ELISA) and immunoblotting. The binding ability of the proteins to transmissible gastroenteritis virus (TGEV), a porcine coronavirus, was analyzed by ELISA. The inhibitory effect of these proteins to cell infection by TGEV was analyzed using plaque assays. Our data indicate that three truncated pAPNs positively reacted with the specific antiserum and the major binding regions of pAPN were limited in regions 36aa-223aa, 349aa-591aa and 592-963aa. The proteins showed discrepant binding activity to either pAPN antibody or TGE virions. Moreover, the truncated proteins blocked the infection of cells by TGEV to different extent. The results suggest that the major antibody-binding domains of pAPN may associate with the receptor-binding determinants. The role of APN is discussed in the context of virus receptor usage.

Citations

May 3, 2011·Hybridoma·Siqingaowa Suo, Xiaofeng Ren
Oct 12, 2013·Monoclonal Antibodies in Immunodiagnosis and Immunotherapy·Donghua GuoDongbo Sun
May 31, 2011·Expert Opinion on Therapeutic Patents·Li SuWenfang Xu
Oct 14, 2018·Transgenic Research·Kristin M WhitworthRandall S Prather
Jul 13, 2021·Veterinary Research Communications·Qiang Liu, Huai-Yu Wang

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Methods Mentioned

BETA
ELISA
PCR
electrophoresis
transfection

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