Al. Bisno et al., M-PROTEINS OF GROUP-C STREPTOCOCCI ISOLATED FROM PATIENTS WITH ACUTE PHARYNGITIS, Journal of clinical microbiology, 34(10), 1996, pp. 2511-2515
We studied 15 strains of group C streptococci (Streptococcus equisimil
is) isolated from the throats of college students with acute pharyngit
is and 5 strains isolated from patients with noninfectious problems. N
ineteen of the 20 strains resisted phagocytic killing during incubatio
n in normal human blood, suggesting that they might express M proteins
, Genomic DNA from all 20 strains hybridized with a probe correspondin
g to the carboxyterminal one-third of the group A M-protein gene emm24
, a region that is highly conserved among M proteins of group A and gr
oup G streptococci, The DNA sequences of the N-terminal (variable) reg
ions of the M-protein-encoding genes from two disease-associated group
C isolates and one control isolate were determined, The predicted ami
no acid sequences of the two pharyngitis strains were identical and we
re 88% homologous to the amino acid sequence of a group G M-protein ge
ne. The predicted terminal amino acid sequence of the control strain d
oes not correspond to any such sequences in the GenBank database, All
three strains studied possess the conserved region domain common to cl
ass I group A hi-protein types epidemiologically associated with rheum
atic fever. These studies demonstrate the presence of M proteins in st
rains of S. equisimilis isolated in cases of endemically occurring acu
te pharyngitis. Certain of these proteins are similar to those of grou
p G streptococci, while others may represent new M types, The similari
ty in structure and function between M proteins of nonrheumatogenic se
rogroups and those of rheumatogenic group A streptococci suggests that
factors other than or in addition to M protein per se are likely invo
lved in the pathogenesis of rheumatic fever.