Evidence of VP1 of duck hepatitis A type 1 virus as a target of neutralizing antibodies and involving receptor-binding activity.
The VP1 protein of the foot-and-mouth disease virus (FMDV) is a major target of neutralizing antibodies and is responsible for viral attachment to permissive cells via an RGD motif. VP1 of duck hepatitis A type 1 virus (DHAV-1) does not contain any RGD motif. To investigate the antibody and receptor-binding properties of DHAV-1, VP1 has been expressed as a His fusion protein (His-VP1) in baculovirus system. Sera against His-VP1 raised in rabbits effectively neutralized DHAV-1 infection in vitro and in vivo. A flow cytometry binding assay indicated that His-VP1 bound to duck embryo fibroblast cell (DEF) surface receptors. This binding was reduced in a dose-dependent manner by the addition of purified DHAV-1 virions, demonstrating the specificity of this interaction. A separate cell-binding assay also implicated His-VP1 in receptor binding. Importantly, anti-His-VP1 antibodies inhibited the binding of DHAV-1 virions to DEF cells, suggesting that these antibodies exert their neutralizing activity by blocking viral attachment. Similar to the counterpart of FMDV, DHAV-1 VP1 appears to be involved in receptor binding activity and a target of protective antibodies. This study confirms the potential of recombinant VP1 protein to serve as vaccine and diagnostic reagents for the control of DHAV-1 infections.
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of the Chinese Academy of Agricultural Sciences, Harbin, 150001, China.
Xiaojun
X
Li
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of the Chinese Academy of Agricultural Sciences, Harbin, 150001, China.
Ran
R
Zhao
College of Food and Bioengineering, Qiqihar University, Qiqihar, 161006, China.
Wei
W
Lin
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of the Chinese Academy of Agricultural Sciences, Harbin, 150001, China.
Chenxi
C
Li
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of the Chinese Academy of Agricultural Sciences, Harbin, 150001, China.
Tingting
T
Zhang
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of the Chinese Academy of Agricultural Sciences, Harbin, 150001, China.
Fanyi
F
Meng
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of the Chinese Academy of Agricultural Sciences, Harbin, 150001, China. Electronic address: liuming04@126.com.
Ming
M
Liu
State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute of the Chinese Academy of Agricultural Sciences, Harbin, 150001, China. Electronic address: yunzhang03@yahoo.com.
Yun
Y
Zhang
D000818:Animals; D057134:Antibodies, Neutralizing / Q000276:immunology*; D002460:Cell Line; D002478:Cells, Cultured; D003001:Cloning, Molecular; D004372:Ducks; D015870:Gene Expression; D006508:Hepatitis Antibodies / Q000276:immunology*; D004371:Hepatitis Virus, Duck / Q000502:physiology*; D006524:Hepatitis, Viral, Animal / Q000276:immunology / Q000821:virology; D006801:Humans; D011485:Protein Binding; D011991:Receptors, Virus / Q000378:metabolism*; D011993:Recombinant Fusion Proteins; D015678:Viral Structural Proteins / Q000235:genetics / Q000276:immunology* / Q000378:metabolism*; D053585:Virus Attachment
D057134:Antibodies, Neutralizing; D006508:Hepatitis Antibodies; D011991:Receptors, Virus; D011993:Recombinant Fusion Proteins; D015678:Viral Structural Proteins
Duck hepatitis A type 1 virus; Neutralizing antibody; Receptor; VP1 protein