TY - JOUR
T1 - Identification of antigens for the development of a subunit vaccine against Photobacterium damselae ssp. piscicida
AU - Ho, Li Ping
AU - Han-You Lin, John
AU - Liu, Hsiao Chien
AU - Chen, Huey En
AU - Chen, Tzong-Yueh
AU - Yang, Huey Lang
PY - 2011/1/1
Y1 - 2011/1/1
N2 - Photobacterium damselae ssp. piscicida (Ph.d.p.), the causative agent of photobacteriosis, is among the most important pathogens affecting finfish aquaculture globally. With the emergence of recombinant technology, subunit vaccines have been actively pursued, but mostly for viral diseases. Bacterial subunit vaccines are more difficult to develop since the bacterial genome is more complex, with numerous candidate antigens, leading to a lengthy and laborious screening process. Immunoproteomics, using western blotting on protein analyzed with 2DE and LC-MS/MS to isolate immune-reactive proteins and acquire amino acid sequences, followed by recombinant technology to clone the candidate gene, identified eight candidate antigens from Ph.d.p., which have been cloned and expressed in Escherichia coli BL21(DE3). These proteins were purified and used as antigens in an efficacy trial. Three, rHSP60, rENOLASE, and rGAPDH proteins, elicited higher specific antibody titers and stronger protective immunity than the other five and an inactivated Ph.d.p. whole bacterial vaccine. These three antigens may be candidates for the development of a subunit vaccine against Ph.d.p.
AB - Photobacterium damselae ssp. piscicida (Ph.d.p.), the causative agent of photobacteriosis, is among the most important pathogens affecting finfish aquaculture globally. With the emergence of recombinant technology, subunit vaccines have been actively pursued, but mostly for viral diseases. Bacterial subunit vaccines are more difficult to develop since the bacterial genome is more complex, with numerous candidate antigens, leading to a lengthy and laborious screening process. Immunoproteomics, using western blotting on protein analyzed with 2DE and LC-MS/MS to isolate immune-reactive proteins and acquire amino acid sequences, followed by recombinant technology to clone the candidate gene, identified eight candidate antigens from Ph.d.p., which have been cloned and expressed in Escherichia coli BL21(DE3). These proteins were purified and used as antigens in an efficacy trial. Three, rHSP60, rENOLASE, and rGAPDH proteins, elicited higher specific antibody titers and stronger protective immunity than the other five and an inactivated Ph.d.p. whole bacterial vaccine. These three antigens may be candidates for the development of a subunit vaccine against Ph.d.p.
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U2 - 10.1016/j.fsi.2010.11.029
DO - 10.1016/j.fsi.2010.11.029
M3 - Article
C2 - 21134466
AN - SCOPUS:78650690621
VL - 30
SP - 412
EP - 419
JO - Fish and Shellfish Immunology
JF - Fish and Shellfish Immunology
SN - 1050-4648
IS - 1
ER -