Role of M protein in pharyngeal colonization by group A streptococci in rats.
As the initial step in infection, group A streptococci (GAS) colonize either the nasopharyngeal mucosa or the skin of humans. A number of virulence factors have been implicated in the colonization phase of pathogenesis based upon their in vitro activities, but the in vivo data supporting their role in colonization of the host tissues is lacking. In this investigation, the potential requirement for M protein in pharyngeal colonization by GAS was explored by using near-isogenic strains in experimental animals studies. Fischer rats were infected by intranasal and oral inoculation with both M-positive and M-negative Streptococcus pyogenes strains. Colonization of the pharyngeal area by the streptococci was monitored at various time intervals. Both M-positive and M-negative strains colonized during the first week following infection, indicating that M protein was not necessary for this initial colonization. Two M-positive strains of S. pyogenes were recovered from the rats up to 23 weeks following inoculation, while the colonization levels for M-negative strains decreased rapidly in the second and third weeks, becoming negligible by the fourth week. This indicates a potential role for M protein in the persistence of colonization at this mucosal surface. Colonization of rats with either M-positive strain of S. pyogenes also resulted in the appearance of salivary and serum antibody responses. This in vivo model should allow further investigation into factors required for GAS disease, including the examination of the potential role of the host immune response both in modulation of the pharyngeal surface and in modulation of antigenic changes in M protein or other surface factors.
Department of Microbiology, University of Alabama, Birmingham 35294.
S K
SK
Hollingshead
J W
JW
Simecka
S M
SM
Michalek
D018829:Adhesins, Bacterial; D000818:Animals; D000942:Antigens, Bacterial; D000954:Antigens, Surface / Q000502:physiology; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000276:immunology; D002352:Carrier Proteins; D010450:Endopeptidases / Q000502:physiology; D005260:Female; D009092:Mucous Membrane / Q000382:microbiology; D010614:Pharynx / Q000382:microbiology*; D051381:Rats; D011916:Rats, Inbred F344; D013045:Species Specificity; D013297:Streptococcus pyogenes / Q000472:pathogenicity*
D018829:Adhesins, Bacterial; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; C014689:streptococcal M protein; D010450:Endopeptidases; C053088:C5a peptidase