PMID- 2456272
OWN - NLM
STAT- MEDLINE
DA  - 19880831
DCOM- 19880831
LR  - 20091118
IS  - 0019-9567 (Print)
IS  - 0019-9567 (Linking)
VI  - 56
IP  - 8
DP  - 1988 Aug
TI  - Conservation of protective and nonprotective epitopes in M proteins of group A
      streptococci.
PG  - 2198-204
AB  - Carefully controlled hybridization experiments with probes from a cloned serotype
      5 M protein (M5) gene (smp5) were performed with DNA isolated from heterologous M
      types of group A streptococci, and the homologies detected by hybridization were 
      compared with the ability of anti-pepM5 serum to cross-opsonize heterologous M
      types. As previously reported (J.R. Scott, S.K. Hollingshead, and V.A. Fischetti,
      Infect. Immun. 52:609-612, 1986), extensive structural homologies exist among the
      3' ends of heterologous M protein genes, but there appears to be an increase in
      sequence variation as one moves towards the 5' ends. However, a clear, predictive
      correlation between the hybridization patterns and cross-opsonization was not
      observed. Antibodies raised to a synthetic peptide corresponding to central,
      conserved sequences adjacent to the C-terminal sides of the pepsin cleavage sites
      in M5, serotype 6 M protein, and serotype 24 M protein cross-reacted with
      heterologous acid-extracted M antigens but were not protective and did not bind
      to intact streptococcal cells, indicating that these epitopes are inaccessible on
      the intact cell surface. Removal of the N-terminal half of M5, serotype 6 M
      protein, or serotype 24 M protein by pepsin exposed the conserved epitope on the 
      cell surface. These results suggest that immunoaccessible protective epitopes are
      confined to the highly variable N-terminal halves of M proteins and that a
      single, broadly conserved protective M protein epitope does not exist.
AD  - Department of Microbiology, Medical School, University of Newcastle upon Tyne,
      England.
FAU - Miller, L
AU  - Miller L
FAU - Burdett, V
AU  - Burdett V
FAU - Poirier, T P
AU  - Poirier TP
FAU - Gray, L D
AU  - Gray LD
FAU - Beachey, E H
AU  - Beachey EH
FAU - Kehoe, M A
AU  - Kehoe MA
LA  - eng
GR  - AI10085/AI/NIAID NIH HHS/United States
GR  - AI15619/AI/NIAID NIH HHS/United States
GR  - Wellcome Trust/United Kingdom
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - UNITED STATES
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Antigens, Bacterial)
RN  - 0 (Bacterial Outer Membrane Proteins)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Epitopes)
RN  - 0 (streptococcal M protein)
SB  - IM
MH  - Amino Acid Sequence
MH  - Antigens, Bacterial/*immunology
MH  - *Bacterial Outer Membrane Proteins
MH  - Bacterial Proteins/genetics/*immunology
MH  - *Carrier Proteins
MH  - Cross Reactions
MH  - Epitopes
MH  - Genes
MH  - Genes, Bacterial
MH  - Molecular Sequence Data
MH  - Sequence Homology, Nucleic Acid
MH  - Streptococcus pyogenes/*immunology
MH  - Structure-Activity Relationship
PMC - PMC259545
OID - NLM: PMC259545
EDAT- 1988/08/01
MHDA- 1988/08/01 00:01
CRDT- 1988/08/01 00:00
PST - ppublish
SO  - Infect Immun. 1988 Aug;56(8):2198-204.