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PubMed1979

Purification of a streptococcal bacteriocin (viridin B) and its separation from alpha-hemolysin.

Viridin B, a bacteriocin produced by Streptococcus mitis, copurified with the alpha-hemolysin after ammonium sulfate precipitation and gel filtration on Sephadex G-200. The bacteriocin and hemolysin were separated in some instances by ion-exchange chromatography on diethylaminoethyl-Sephadex A-50, but the two substances were shown to be distinct after polyacrylamide gel electrophoresis. Attempts at recovery of nonhemolytic or nonbacteriocinogenic mutants were unsuccessful after exposure to mutagenic agents. The molecular weight of viridin B was determined to be approximately 87,000.

Bacterial Proteins↗

PubMed1984

Reduction of the susceptibility to infective endocarditis with time in animals with endocavitary catheters.

In a previous study we showed that the lesions of non-bacterial thrombotic endocarditis induced by means of implantation of a catheter in the left ventricle (LV) of the rabbit, undergo inner connectivization and surface endothelialization, which are completed within 2-3 months. In the present study we have investigated whether these histological changes lead to a variation in susceptibility to infective endocarditis (IE). After studying two control groups, we compared the incidence of IE in four groups of 15 rabbits each, inoculated with Streptococcus mitis I, 10, 35 and 70 days after implantation of a catheter in the LV. The frequency of infection was shown to be progressively reduced from 100% to 26.7%. This demonstrates that endothelialization of the catheter and the sterile vegetations protect the animals from IE.

Animals↗

PubMed1981

Effect of human saliva on glucose uptake by Streptococcus mutans and other oral microorganisms.

We examined the effects of human whole salivary supernatant and parotid fluid on glucose uptake by Streptococcus mutans, Streptococcus sanguis, Streptococcus mitis, Actinomyces viscosus, Staphylococcus aureus, and Escherichia coli. The following three effects of saliva were observed: (i) inhibition of glucose uptake (S. mutans, S. sanguis), (ii) promotion of a transient, rapid (0 to 30 s) burst of glucose uptake (S. mutans, S. sanguis), and (iii) enhancement of glucose uptake (S. mitis, A. viscosus, S. aureus, E. coli). We observed no differences between the effects of whole salivary supernatant and the effects of parotid fluid. Heat treatment (80 degrees C, 10 min) of saliva or the addition of dithiothreitol abolished inhibition of glucose uptake. Supplementation of saliva with H(2)O(2) potentiated inhibition of glucose uptake. S. mitis and A. viscosus, which were stimulated by saliva alone, were inhibited by H(2)O(2)-supplemented saliva; 50% inhibition of glucose uptake by S. mutans and S. mitis required ca. 10 muM H(2)O(2) in 50% (vol/vol) saliva. Loss of the inhibitory action of saliva occurred at about 5% (vol/vol) saliva. Supplementation of saliva dilutions with SCN(-) and H(2)O(2) extended the inhibitory activity to solutions containing ca. 0.2% (vol/vol) saliva. We suggest that the salivary lactoperoxidase-SCN(-)-H(2)O(2) system is responsible for the inhibitory activity of saliva reported here. Furthermore, we concluded that lactoperoxidase and SCN(-) are present in saliva specimens in concentrations that exceed minimal inhibitory levels by factors of ca. 500 and 10 to 20, respectively. The resistance of A. viscosus, S. aureus, and E. coli to the inhibitory potential of saliva alone was probably due to the production of catalase by these organisms. The resistance of S. mitis may have been due to special effects of saliva on H(2)O(2) accumulation by this organism compared with S. mutans and S. sanguis. The basis of saliva-dependent enhancement of glucose uptake and the basis of promotion of a transient, rapid burst of glucose uptake are unknown. The role of the salivary lactoperoxidase-SCN(-)-H(2)O(2) system in the oral microbial ecosystem is discussed.

Actinomyces↗

PubMedDate not supplied

[Phlegmon of the fore arm succeeding to a dog-bite : respective role of the miscellaneous bacteria involved in this mixed infection (author's transl)].

The authors report a case of a severe mixed infection (phlegmon of the fore arm) succeeding to a dog bite. A complex flora has been isolated from this phlegmom : Pasteurella multocida, Pasteurella pneumotropica, Streptococcus mitis, Actinomyces sp., Bacteroides melaninogenicus, and a Gram- bacteria related to group II j. The pathogeny of such diseases is discussed, dwelling in one hand on the part of synergistic development of these various germs and in the other hand on the part played by saliva in the severity of animal or human bites. This kind of wound requires careful disinfection and radical debridment without omitting a preventive broad-spectrum antibiotherapy.

Actinomyces↗

PubMed1994

Mosaic pbpX genes of major clones of penicillin-resistant Streptococcus pneumoniae have evolved from pbpX genes of a penicillin-sensitive Streptococcus oralis.

Penicillin-resistant clinical isolates of Streptococcus pneumoniae contain mosaic penicillin-binding protein (PBP) genes that encode PBPs with decreased affinity for beta-lactam antibiotics. The mosaic blocks are believed to be the result of gene transfer of homologous PBP genes from related penicillin-resistant species. We have now identified a gene homologous to the pneumococcal PBP2x gene (pbpX) in a penicillin-sensitive Streptococcus oralis isolate M3 from South Africa that diverged by almost 20% from pbpX of penicillin-sensitive pneumococci, and a central sequence block of a mosaic pbpX gene of Streptococcus mitis strain NCTC 10712. In contrast, it differed by only 2-4% of the 1 to 1.5 kb mosaic block in pbpX genes of three genetically unrelated penicillin-resistant S. pneumoniae isolates, two of them representing clones of serotype 6B and 23F, which are prevalent in Spain and are also already found in other countries. With low concentrations of cefotaxime, transformants of the sensitive S. pneumoniae R6 strain could be selected containing pbpX genes from either S. mitis NCTC 10712 or S. oralis M3, demonstrating that genetic exchange can already occur between beta-lactam-sensitive species. These data are in agreement with the assumption that PBPs as penicillin-resistance determinants have evolved by the accumulation of point mutations in genes of sensitive commensal species.

Amino Acid Sequence↗

PubMed2000

Immunoglobulins in nasal secretions of healthy humans: structural integrity of secretory immunoglobulin A1 (IgA1) and occurrence of neutralizing antibodies to IgA1 proteases of nasal bacteria.

Certain bacteria, including overt pathogens as well as commensals, produce immunoglobulin A1 (IgA1) proteases. By cleaving IgA1, including secretory IgA1, in the hinge region, these enzymes may interfere with the barrier functions of mucosal IgA antibodies, as indicated by experiments in vitro. Previous studies have suggested that cleavage of IgA1 in nasal secretions may be associated with the development and perpetuation of atopic disease. To clarify the potential effect of IgA1 protease-producing bacteria in the nasal cavity, we have analyzed immunoglobulin isotypes in nasal secretions of 11 healthy humans, with a focus on IgA, and at the same time have characterized and quantified IgA1 protease-producing bacteria in the nasal flora of the subjects. Samples in the form of nasal wash were collected by using a washing liquid that contained lithium as an internal reference. Dilution factors and, subsequently, concentrations in undiluted secretions could thereby be calculated. IgA, mainly in the secretory form, was found by enzyme-linked immunosorbent assay to be the dominant isotype in all subjects, and the vast majority of IgA (median, 91%) was of the A1 subclass, corroborating results of previous analyses at the level of immunoglobulin-producing cells. Levels of serum-type immunoglobulins were low, except for four subjects in whom levels of IgG corresponded to 20 to 66% of total IgA. Cumulative levels of IgA, IgG, and IgM in undiluted secretions ranged from 260 to 2,494 (median, 777) microg ml(-1). IgA1 protease-producing bacteria (Haemophilus influenzae, Streptococcus pneumoniae, or Streptococcus mitis biovar 1) were isolated from the nasal cavities of seven subjects at 2.1 x 10(3) to 7.2 x 10(6) CFU per ml of undiluted secretion, corresponding to 0.2 to 99.6% of the flora. Nevertheless, alpha-chain fragments characteristic of IgA1 protease activity were not detected in secretions from any subject by immunoblotting. Neutralizing antibodies to IgA1 proteases of autologous isolates were detected in secretions from five of the seven subjects but not in those from two subjects harboring IgA1 protease-producing S. mitis biovar 1. alpha-chain fragments different from Fc(alpha) and Fd(alpha) were detected in some samples, possibly reflecting nonspecific proteolytic activity of microbial or host origin. These results add to previous evidence for a role of secretory immunity in the defense of the nasal mucosa but do not help identify conditions under which bacterial IgA1 proteases may interfere with this defense.

Adult↗

PubMed1994

Bacterial colonization and degradation of demineralized dentin matrix in situ.

Lesion formation in dentin involves demineralization followed by degradation of the exposed organic matrix. Proteinases from microorganisms present in the dentin are believed to play an important role in the breakdown of the dentinal collagen. In this study, the microflora colonizing decalcified dentin matrix, placed in situ, was identified. The gelatinolytic activity of the isolated strains was assessed and related to the degradation of the dentin matrix. The predominant species found were Streptococcus mitis. Peptostreptococcus productus, Lactobacillus casei, Propionibacterium species and Veillonella parvula. Marked interindividual variation in the composition of the microflora was observed. The microflora possessed gelatinolytic activity, although no correlation was found with the severity of dentin matrix degradation. The chemically determined loss of collagen varied between 0 and 67 wt% per participant and corresponded with the extent of collagen degradation observed by transmission electron microscopy.

Animals↗

PubMed2002

Infections caused by viridans streptococci in patients with neutropenia.

The frequency of isolation of viridans streptococci from the blood of neutropenic patients with cancer has significantly increased over the course of the last 10-15 years. Risk factors in this patient population include severe neutropenia, oral mucositis, administration of high-dose cytosine arabinoside, and antimicrobial prophylaxis with either trimethoprim-sulfamethoxazole or a fluoroquinolone. In some patients with cancer and neutropenia who develop viridans streptococcal bacteremia, a toxic shock-like syndrome has been described; Streptococcus mitis has been the causative species in most cases. Because resistance of viridans streptococci to a variety of antimicrobial agents is increasingly recognized, penicillin susceptibility cannot be assumed, and empirical vancomycin therapy should be used to treat neutropenic patients with cancer who have shock or are developing acute respiratory distress syndrome. Given the seriousness of septicemia caused by viridans streptococci and the potential for selection of other resistant microorganisms, the routine practice of antimicrobial prophylaxis for neutropenic patients with cancer should be reconsidered.

Anti-Bacterial Agents↗

PubMed1963

NORMAL FLORA OF THE NOSE, THROAT, AND LOWER INTESTINE OF DOGS.

Clapper, W. E. (The Lovelace Foundation for Medical Education and Research, Albuquerque, N.M.) and G. H. Meade. Normal flora of the nose, throat, and lower intestine of dogs. J. Bacteriol. 85:643-648. 1963.-An attempt was made to isolate and identify the complete normal flora of the rectum, nose, and throat of beagles. For primary isolation, 12 different kinds of media were used. Incubation of blood agar plates and slants anaerobically, and of thioglycolate broth aerobically, allowed the growth of obligate anaerobes. From the rectal specimens, 20 species of bacteria and 10 species of fungi were isolated and identified. The organisms were similar to those found in the human intestine. Escherichia coli, Streptococcus mitis, enterococci, S. lactis, Bacillus species, and coliforms other than E. coli were most frequently encountered. The frequency of occurrence was approximately the same at both samplings in more commonly cultured bacteria. Pathogenic E. coli were isolated from nearly one-third of the first specimens. These were the only human pathogens observed. In the throat cultures, 29 species of bacteria and 2 species of yeasts were identified, and 27 species of bacteria were identified from the nasal cultures. S. mitis, Neisseria, and coagulase-negative Staphylococcus were most often isolated. The flora was similar to that found in human nose and throat cultures, except that more Haemophilus and pneumococcus and fewer coliforms are generally found in human throats. Organisms resembling human pathogens were group A streptococci and coagulase-positive staphylococci. These were isolated infrequently. It appears that this kind of examination would reveal any significant changes in normal flora that might be related to the health of the animal.

Animals↗

PubMed1992

Antimicrobial resistance in Streptococcus pneumoniae: a South African perspective.

Resistance to penicillin among South African strains of Streptococcus pneumoniae increased from 4.9% in 1979 to 14.4% in 1990. Except for resistance to co-trimoxazole (44%), resistance to other antimicrobial agents remained relatively low. Multiply resistant strains belonged mainly to serovars 6B, 19A, 14, and, more recently, 23F. Use of chloramphenicol to treat meningitis caused by strains relatively resistant to penicillin proved to be unsatisfactory, probably because of the inadequate bactericidal activity of chloramphenicol against these strains. Spread of penicillin-resistant nasopharyngeal strains in pediatric wards was most common among children who received antimicrobial therapy. Penicillin-binding protein (PBP) patterns were shown to vary in resistant clinical strains. Interspecies transfer of penicillin resistance between Streptococcus mitis and S. pneumoniae was demonstrated and antigenic homology was found in PBPs 1A and 2B of strains belonging to these species. Restriction enzyme mapping following DNA amplification of the PBP 2B gene revealed six arrangements among South African strains within serogroup 19. Despite extensive studies in South Africa and several other countries, many questions with regard to the global problem of antimicrobial resistance among S. pneumoniae strains remain unanswered, especially those that relate to prevalence in developing regions of the world.

Carrier State↗

PubMed1993

Inhibition of platelet binding and aggregation by streptococcal exopolysaccharide.

Streptococcal exopolysaccharides are major virulence factors in the pathogenesis of endocarditis. They promote bacterial adherence to valves and subsequent vegetation formation. Since platelet binding and aggregation by streptococci are postulated mechanisms for endocardial colonization and vegetation production, the effect of exopolysaccharide on binding and aggregation was evaluated by flow cytometry and aggregometry. Streptococcus salivarius D1, a minimal exopolysaccharide producer, bound human platelets extensively (86.8% of bacteria bound by 1 min). S. Salivarius M13 and M15 and Streptococcus mitis M4 produced larger amounts of exopolysaccharide and bound platelets significantly less (52.6%, 51.2%, 52.8%, respectively). Exopolysaccharide also inhibited platelet aggregation: Strains with minimal exopolysaccharide aggregated platelets maximally, while strains with extensive exopolysaccharide failed to induce aggregation. Removal of exopolysaccharide by shearing restored aggregation by these latter strains. Thus, exopolysaccharides can inhibit the binding and aggregation of platelets by streptococci. The virulence associated with exopolysaccharide may result from the inhibition of platelet-mediated interactions that limit disease progression.

Blood Platelets↗

PubMed2006

Use of the Phoenix automated system for identification of Streptococcus and Enterococcus spp.

The Phoenix system (Becton Dickinson Diagnostic Systems, Sparks, MD) was evaluated for identification (ID) to the species level of streptococci and enterococci. Two hundred clinical isolates were investigated: beta-hemolytic streptococci (n = 50), Streptococcus pneumoniae organisms (n = 46), viridans group streptococci (n = 31), Enterococcus faecium (n = 36), Enterococcus faecalis (n = 25), and other catalase-negative cocci (n = 12). The API system (bioMérieux, Marcy l'Etoile, France) was used as a comparator. Molecular methods (sequencing of 16S rRNA and zwf and gki genes and ddl gene amplification) were used to investigate discordant results. Upon resolution of discrepancies, correct species ID was achieved by the Phoenix system for 121/129 (93.8%) streptococci and 63/70 (90.0%) enterococci. Excellent results were obtained for S. pneumoniae (45/45) and beta-hemolytic streptococci (49/50). With regard to viridans streptococci, the accuracy of the Phoenix system was 83.9%. Among the latter organisms, the best performance was obtained with isolates of the Streptococcus sanguinis group and Streptococcus anginosus group; problems were instead encountered with the Streptococcus mitis group. Four E. faecium and three E. faecalis isolates were misidentified as Enterococcus casseliflavus/Enterococcus gallinarum or Enterococcus durans. Thus, these isolates were identified only at the genus level. Compared with commercially available systems, the Phoenix system appears a reliable diagnostic tool for identifying clinically relevant streptococci and enterococci. The SMIC/ID-2 panel proved particularly effective for beta-hemolytic streptococci and pneumococci.

Automation↗

PubMed1986

Effect of monoclonal antibodies against lipoteichoic acid from the oral bacterium Streptococcus mutans on its adhesion and plaque-accumulation in vitro.

Five monoclonal antibodies directed against Streptococcus mutans strain JBP lipoteichoic acid (LTA) were characterized. They were all similarly reactive with the immunizing LTA-containing extract, with intact Strep. mutans JBP cells and with LTA purified from Lactobacillus casei. Immobilized anti-LTA antibodies removes LTA from LTA-containing extracts. The binding of antibodies to LTA was inhibited by the aqueous extract but not by the organic extract of de-acylated LTA, indicating reactivity with the polyglycerol-phosphate portion of the molecule. Antibodies were reactive with all serotypes of Strep. mutans, as well as with strains of Streptococcus salivarius, Streptococcus sanguis and L. casei, but not with LTA-negative species Streptococcus mitis or Actinomyces viscosus. Anti-LTA antibodies at doses of 0.3 or 3.0 micrograms/ml, had no effect on the adherence of Strep. mutans JBP to experimental salivary pellicles formed on hydroxyapatite, but enhanced adherence 150-300 per cent at 30 micrograms/ml. There was no effect of anti-LTA antibodies in a chemostat model which measured sucrose-dependent plaque accumulation by Strep. mutans. The results argue against a major role for LTA in Strep. mutans adherence or plaque accumulation in vitro.

Adhesiveness↗

PubMed1997

Pathogenicity of Prevotella intermedia and Prevotella nigrescens isolates in a wound chamber model in rabbits.

The pathogenicity of 14 isolates identified as Prevotella intermedia or Prevotella nigrescens by serogrouping using monoclonal antibodies was compared in a tissue cage model in rabbits. Seven strains from periodontal abscesses, 5 strains from deep periodontal pockets and 2 strains from gingivitis were tested in the animal model comprising 6 Teflon tissue cages implanted on the back each of 34 rabbits. A total of 10(5)-10(8) cells of P. intermedia or P. nigrescens strains were inoculated alone or together with either Actinobacillus actinomycetemcomitans or Streptococcus mitis. Five strains of Porphyromonas gingivalis were used as a reference. The infectivity was recorded as pus formation and log viable count in aspirated material for 3, 7 and 14 days. None of the Prevotella strains inoculated in monoculture survived more than 3 days, and they had no capacity to produce abscess. P. intermedia or P. nigrescens strains in combination with A. actinomycetemcomitans produced abscesses in 33-100% and with S. mitis in 42-100%. No difference in abscess formation or log viable count in samples after 14 days was recorded between serogroup I (P. intermedia) and serogroup II and III (P. nigrescens). The infectivity of P. intermedia or P. nigresceas strains did not differ whether they were isolated from periodontal abscess, periodontal pocket or gingivitis. P. intermedia and P. nigrescens strains produced abscesses in combination with a facultative anaerobic strain and appears to have a similar pathogenicity in the wound chamber model in rabbits.

Aggregatibacter actinomycetemcomitans↗

PubMed1999

Streptococcal histone induces murine macrophages To produce interleukin-1 and tumor necrosis factor alpha.

The histone-like protein (HlpA) is highly conserved among streptococci. After lysis of streptococci in infected tissues, HlpA can enter the bloodstream and bind to proteoglycans in the glomerular capillaries of kidneys, where it can react with antibodies or stimulate host cell receptors. Deposits of streptococcal antigens in tissues have been associated with localized acute inflammation. In this study, we measured the ability of purified HlpA (5 to 100 microg/ml), from Streptococcus mitis, to induce the production of proinflammatory cytokines by cultured, murine peritoneal macrophages. The release of tumor necrosis factor alpha (TNF-alpha) and interleukin-1 (IL-1) was time and concentration dependent and was not diminished by the presence of polymyxin B. Exposure of macrophages to a mixture of HlpA and lipoteichoic acid resulted in a synergistic response in the production of both TNF-alpha and IL-1. Stimulation with a mixture of HlpA and heparin resulted in reduced cytokine production (50% less IL-1 and 76% less TNF-alpha) compared to that by cells incubated with HlpA alone. The inclusion of antibodies specific to HlpA in macrophage cultures during stimulation with HlpA did not affect the quantity of TNF-alpha or IL-1 produced. These observations suggest that streptococcal histone may contribute to tissue injury at infection sites by promoting monocytes/macrophages to synthesize and release cytokines that initiate and exacerbate inflammation. Streptococcus pyogenes, which can infect tissues in enormous numbers, may release sufficient amounts of HlpA to reach the kidneys and cause acute poststreptococcal glomerulonephritis.

Animals↗

PubMed2003

Amino acid sequence requirements in the hinge of human immunoglobulin A1 (IgA1) for cleavage by streptococcal IgA1 proteases.

The amino acid sequence requirements in the hinge of human immunoglobulin A1 (IgA1) for cleavage by IgA1 proteases of different species of Streptococcus were investigated. Recombinant IgA1 antibodies were generated with point mutations at proline 227 and threonine 228, the residues lying on either side of the peptide bond at which all streptococcal IgA1 proteases cleave wild-type human IgA1. The amino acid substitutions produced no major effect upon the structure of the mutant IgA1 antibodies or their functional ability to bind to Fcalpha receptors. However, the substitutions had a substantial effect upon sensitivity to cleavage with some streptococcal IgA1 proteases, with, in some cases, a single point mutation rendering the antibody resistant to a particular IgA1 protease. This effect was least marked with the IgA1 protease from Streptococcus pneumoniae, which showed no absolute requirement for either proline or threonine at residues 227 to 228. By contrast, the IgA1 proteases of Streptococcus oralis, Streptococcus sanguis, and Streptococcus mitis had an absolute requirement for proline at 227 but not for threonine at 228, which could be replaced by valine. There was evidence in S. mitis that proteases from different strains may have different amino acid requirements for cleavage. Remarkably, some streptococcal proteases appeared able to cleave the hinge at a distant alternative site if substitution prevented efficient cleavage of the original site. Hence, this study has identified key residues required for the recognition of the IgA1 hinge as a substrate by streptococcal IgA1 proteases, and it marks a preliminary step towards development of specific enzyme inhibitors.

Amino Acid Sequence↗

PubMed1998

Structural integrity of infant salivary immunoglobulin A (IgA) in IgA1 protease-rich environments.

IgA1 protease-secreting Streptococcus mitis often dominate the oral flora of the neonate and young infant at a time when salivary IgA concentrations are low and usually enriched in the secretory IgA1 subclass. To study the possible influence of these degradative enzymes on emerging host immunity, the presence of IgA1 protease-secreting streptococci was related to the structural integrity of salivary IgA in 24 infants who were between 3 and 18 weeks of age. At least one IgA1 protease-secreting strain could be isolated from the oral mucosa of 79% of the infants and comprised a mean of 38% of the total streptococcal flora of these infants. Chromatographic analyses of resting whole saliva from 16 infants revealed, however, that 95% of the secretory IgA (range 88-100%) remained intact, indicating that minimal immediate IgA proteolysis occurred in the bulk salivary phase. Proteolysis of infant salivary IgA, presumably by indigenous IgA1 protease, could be observed after extended (more than 7 h) in situ incubation of whole saliva at 37 degrees C. Salivary IgA antibody activities to S. mitis components were demonstrated by Western blot in infants colonized with an IgA1 protease-secreting flora. Preliminary evidence suggested that salivary antibody activity in some infants may be directed to IgA1 protease. Thus, the infant's antibody defenses not only appear very early in life but are substantively intact in the bulk salivary phase, even when the oral cavity is colonized with IgA1 protease-secreting streptococcal flora.

Blotting, Western↗

PubMed1979

Chemical composition of Streptococcus mutans cell walls and their susceptibility to Flavobacterium L-11 enzyme.

The susceptibility to a cell wall lytic L-11 enzyme from Flavobacterium sp. and the quantitative and/or qualitative composition of the cell walls of some strains of cariogenic Streptococcus mutans and a non-cariogenic strain of Streptococcus mitis were determined. The purified cell walls of S. mutans strains HS-1 (serotype a), BHT (b), NCTC10449 (c), C67-1 (c), C67-25 (c), OMZ 176 (d), MT703 (e), MT557 (f), OMZ65 (g), and AHT (g), and S. mitis CHT contained glutamic acid, alanine, and lysine as well as muramic acid and glucosamine as a peptidoglycan component. Besides these amino acids, significant amounts of threonine were detected in strains HS-1, OMZ65, and AHT cell walls, and considerable amounts of aspartic acid and/or threonine as well as several other amino acids in OMZ176, OMZ65, and CHT cell walls. Rhamnose was a common special component of the cell walls of S. mutans strains BHT, NCTC10449, MT703, B2 (e), MT557, and AHT, and S. mitis CHT. An additional sugar component, glucose, was detected in the cell walls of all of these strains except BHT, and galactose was found in BHT, AHT, and CHT cell walls. Galactosamine was present in S. mitis CHT cell walls. Varying amounts of phosphorus were detected in the cell walls of all the strains examined. The cell walls of all these streptococcal strains except MT703, 6715, and AHT were susceptible to the lytic action of the L-11 enzyme to various extents. No consistent relationship was observed between the amino acid and sugar composition of these cell walls and their susceptibility to the L-11 enzyme. The chemical composition of these cell walls is discussed in terms of the serological classification of S. mutans.

Amino Acids↗