Expression and immunological comparison of recombinant 35 kDa fragment and full-length recombinant of VP2 proteins of canine parvovirus using escherichia coli expression system

Name: Natnaree Inthong

LCSH: Kasetsart University -- Dissertations. Ph.D. (Agricultural Biotechnology) 2021

Classification :.LCCS: QR408.2.C35

LCSH: Kasetsart University. -- Interdisciplinary Graduate Program -- Dissertations

LCSH: Canine parvovirus

LCSH: Escherichia coli

LCSH: Gene expression.

LCSH: Veterinary vaccines

LCSH: Recombinant proteins

Abstract: Canine parvovirus (CPV) is one of the most common virus infections in young dogs that causes acute hemorrhagic gastroenteritis, leukopenia, nausea, diarrhea and sometimes fatal myocarditis. Currently, there are three genotypic variants (CPV-2a, CPV-2b, and CPV2c) which differs at the amino acid position 426 of VP2 protein. The VP2 capsid protein is the main capsid protein and has been shown to have an important role in the determination of host range of CPV and inducing neutralizing antibody. According to previous study, the circulating CPV in Thailand were 2a and 2b. Nowadays, CPV mutants, including CPV-2c, have been identified in many parts of the world. In this study, eighty five CPV-positive fecal samples were obtained from dogs with either acute hemorrhagic diarrhea or diarrhea. Sixty and 25 CPV positive fecal samples were collected in 2010 and 2018, respectively. Thirtyfour samples were new CPV-2a and 31 samples were new CPV-2b due to amino acids substitution at position 297 (Ser-Ala). In 2018, 5 new CPV-2a, 19 CPV-2c, and 1 feline panleukopenia virus (FPV) were found, but no new CPV-2b was detected. This result showed that the evolution of CPV in Thailand is very dynamic. The recombinant full length and 35 kDa fragment proteins of VP2 gene were expression in Escherichia coli using the pBAD202 Directional TOPO expression system. The optimum concentration of arabinose and time for recombinant full length and 35 kDa fragment proteins of VP2 gene were 0.2% for 6 hours and 0.02% for 6 hours, respectively. The molecular weight of recombinant full length and 35 kDa fragment proteins were 81 and 51 kDa, respectively. Both recombinant full length and 35 kDa fragment proteins were interact specifically with rabbit anti CPV polyclonal antibody. Therefore, the recombinant 35 kDa fragment proteins of VP2 gene may be used for further development of the diagnostic test for the detection of CPV or a vaccine against CPV.

Kasetsart University. Office of the University Library

Address: Bangkok

Email: tdckulib@ku.ac.th

Name: Theerapol Sirinarumitr

Role: Thesis Advisor

Name: Sarawan Kaewmongkol

Role: Thesis CO-Advisor

Created: 2021

Modified: 2025-07-14

Issued: 2025-07-14

วิทยานิพนธ์/Thesis

application/pdf

URL: https://www.lib.ku.ac.th/KUthesis/2564/natnaree-int-all.pdf

CallNumber: QR408.2.C35 .N38

eng

DegreeName: Doctor of Philosophy

Level: Doctoral Degraee

Descipline: Agricultural Biotechnology

Grantor: Kasetsart University

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