S. Bernath et al., Computerized comparison of the protein compositions of Erysipelothrix rhusiopathiae and Erysipelothrix tonsillarum strains, J VET MED B, 48(1), 2001, pp. 73-79
Citations number
21
Categorie Soggetti
Veterinary Medicine/Animal Health
Journal title
JOURNAL OF VETERINARY MEDICINE SERIES B-INFECTIOUS DISEASES AND VETERINARYPUBLIC HEALTH
Protein profiles of six Erysipelothrix rhusiopathiae strains, five Erysipel
othrix tonsillarum strains and three Erysipelothrix strains of uncertain ta
xonomic position were studied by sodium dodecyl sulphate-polyacrylamide gel
electrophoresis (SDS-PAGE). In a computerized comparison of the protein pa
tterns of the strains, the level of similarity between the strains was dete
rmined. The SDS-PAGE protein bands were divided into 14 groups based on mol
ecular weight. The relative distribution of proteins within these groups wa
s used to characterize the strains. These distribution patterns were analys
ed by computing Pearson's correlation coefficient between strains, and by c
luster analysis based on Euclidean distances and the unweighted pair-group
method of arithmetic averages (UPGMA). The geometric mean of the similariti
es calculated by Pearson's correlation coefficient was 0.980 +/- 0.018 betw
een the E. rhusiopathiae strains and 0.979 +/- 0.013 for E. tonsillarum str
ains. The value was 0.932 +/- 0.036 between the strains belonging to differ
ent species. However, a threshold Value applicable for identification of a
given strain to a species could not be established. Of the three strains of
uncertain taxonomic position, the strains designated Rotzunge and Iszap 4
had a protein composition more similar to that of E. tonsillarum than to th
at of the E. rhusiopathiae type strain. The strain designated Pecs 56, whic
h may be a member of a new species according to literature data, gave incon
sistent results Ly the two methods used. The computerized evaluation method
developed here is suitable for the comparison of the protein composition o
f the strains and for thr construction of the protein similarity tree by cl
uster analysis.