TY - JOUR
T1 - Comparative analysis of the phenotypic characteristics of high- and low-virulent strains of Edwardsiella tarda
AU - Wang, Y.
AU - Zhang, X. H.
AU - Austin, B.
PY - 2010/12
Y1 - 2010/12
N2 - Edwardsiella tarda is a causative agent of edwardsiellosis in freshwater and marine fish. Extracellular enzymic, haemolytic, hydrophobic and serum resistance activities, haemagglutination, autoagglutination and siderophores of high- and low- virulent E. tarda strains were examined. The results revealed different haemagglutination, autoagglutination, haemolytic, hydrophobic and serum resistance activities in different strains. Analysis of extracellular proteins (ECPs) and outer membrane proteins (OMPs) demonstrated several major, low molecular weight, virulent-strain-specific proteins, which could be virulence-related. Based on the database search with MALDI-TOF MS data, the closest homologies of the three protein bands Ed1, Ed2 and Ed3 were phosphotransferase enzyme family protein, nitrite reductase [NAD(P)H], large subunit and ATP-dependent Lon protease, respectively. A comparison of pathogenicity of purified lipopolysaccharide (LPS) and lipid A from virulent and avirulent strains demonstrated that LPS was one of the virulence factors of the E. tarda isolates, and lipid A was a biologically active determinant of LPS. © 2010 Blackwell Publishing Ltd.
AB - Edwardsiella tarda is a causative agent of edwardsiellosis in freshwater and marine fish. Extracellular enzymic, haemolytic, hydrophobic and serum resistance activities, haemagglutination, autoagglutination and siderophores of high- and low- virulent E. tarda strains were examined. The results revealed different haemagglutination, autoagglutination, haemolytic, hydrophobic and serum resistance activities in different strains. Analysis of extracellular proteins (ECPs) and outer membrane proteins (OMPs) demonstrated several major, low molecular weight, virulent-strain-specific proteins, which could be virulence-related. Based on the database search with MALDI-TOF MS data, the closest homologies of the three protein bands Ed1, Ed2 and Ed3 were phosphotransferase enzyme family protein, nitrite reductase [NAD(P)H], large subunit and ATP-dependent Lon protease, respectively. A comparison of pathogenicity of purified lipopolysaccharide (LPS) and lipid A from virulent and avirulent strains demonstrated that LPS was one of the virulence factors of the E. tarda isolates, and lipid A was a biologically active determinant of LPS. © 2010 Blackwell Publishing Ltd.
KW - Edwardsiella tarda
KW - Lipid A
KW - Lipopolysaccharides
KW - Pathogenicity
KW - SDS-polyacrylamide gel electrophoresis
UR - http://www.scopus.com/inward/record.url?scp=78649468832&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2761.2010.01204.x
DO - 10.1111/j.1365-2761.2010.01204.x
M3 - Article
C2 - 21091725
SN - 0140-7775
VL - 33
SP - 985
EP - 994
JO - Journal of Fish Diseases
JF - Journal of Fish Diseases
IS - 12
ER -
