scholarly journals CHEMICAL BASIS FOR AN IMMUNOLOGICAL SPECIFICITY OF A STRAIN OF STAPHYLOCOCCUS AUREUS

1963 ◽  
Vol 117 (6) ◽  
pp. 925-935 ◽  
Author(s):  
William G. Juergens ◽  
Arnold R. Sanderson ◽  
Jack L. Strominger

Antisera, prepared against formalin-killed cells of Staphylococcus aureus, strain Copenhagen, agglutinated the cell walls of this strain. The agglutination was inhibited by the teichoic acid from the cell wall of this strain, by any degradation product of this teichoic acid which contained the α-acetylglucosaminyl-ribitol unit, by α-phenyl-acetylglucosaminide, and by N-acetylglucosamine, but not by a large number of other haptens related to the cell wall. In quantitative experiments, however, only 40 to 50 per cent of antibody adsorption to cell wall could be inhibited by teichoic acid or by N-acetylglucosamine. The α-acetylglucosaminyl-ribitol unit in the teichoic acid is, therefore, an important immunological determinant in the cell wall of this strain, although other immunological specificities may also exist. The cell walls were also agglutinated by heterologous antisera prepared against streptococcal Group A carbohydrate or against horse serum azophenyl-ß-acetylglucosaminide. The heterologous agglutination, however, was specific for the ß-acetylglucosaminyl-ribitol units in the teichoic acid.

Biochemistry ◽  
1966 ◽  
Vol 5 (12) ◽  
pp. 3748-3764 ◽  
Author(s):  
Emilio Munoz ◽  
Jean-Marie Ghuysen ◽  
Melina Leyh-Bouille ◽  
Jean-Francois Petit ◽  
Hans Heymann ◽  
...  

Biochemistry ◽  
1965 ◽  
Vol 4 (3) ◽  
pp. 474-485 ◽  
Author(s):  
Jean-Marie Ghuysen ◽  
Donald J. Tipper ◽  
Jack L. Strominger

1962 ◽  
Vol 116 (2) ◽  
pp. 229-245 ◽  
Author(s):  
Stephen I. Morse

The cell walls of an 80/81 strain of Staphylococcus aureus (NYH-6) contain alanine, glycine, glutamic acid, lysine, muramic acid, glucosamine, and ribitol phosphate. 94 per cent of the phosphorus and 41 per cent of the glucosamine are removed by extraction of the cell walls with hot 5 per cent TCA, but significant amounts of the other constituents are not extracted by this procedure. The residue after hot TCA extraction (mucopeptide) is susceptible to lysozyme whereas the intact cell walls are resistant. Staphylococcus aureus cell walls are agglutinated by S. aureus antisera. Agglutination of the cell walls of one S. aureus strain is inhibited by absorption of antisera with cell walls of other S. aureus strains but not by absorption with S. albus cell walls. The ribitol teichoic acid can be isolated from cold TCA extracts of the cell walls. This compound consists almost entirely of ribitol phosphate and glucosamine. The isolated teichoic acid of strain NYH-6 is readily fixed to tanned sheep erythrocytes and these sensitized cells are agglutinated by S. aureus antisera. Cold TCA extracts of cell walls of other strains of S. aureus inhibit hemagglutination whereas extracts of S. albus walls do not. Studies on the inhibition of both hemagglutination and precipitation indicate that the antigenic determinant of S. aureus NYH-6 teichoic acid is ß-N-acetylglucosamine.


2004 ◽  
Vol 48 (10) ◽  
pp. 3749-3757 ◽  
Author(s):  
Jennifer L. Koehl ◽  
Arunachalam Muthaiyan ◽  
Radheshyam K. Jayaswal ◽  
Kerstin Ehlert ◽  
Harald Labischinski ◽  
...  

ABSTRACT The cell wall composition and autolytic properties of passage-selected glycopeptide-intermediate Staphylococcus aureus (GISA) isolates and their parent strains were studied in order to investigate the mechanism of decreased vancomycin susceptibility. GISA had relatively modest changes in peptidoglycan composition involving peptidoglycan interpeptide bridges and somewhat decreased cross-linking compared to that of parent strains. The cell wall phosphorus content of GISA strains was lower than that of susceptible parent strains, indicating somewhat lower wall teichoic acid levels in the GISA strains. Similar to whole cells, isolated crude cell walls retaining autolytic activity of GISA had drastically reduced autolytic activity compared to that of parent strains, and this arose early in the development of the GISA phenotype. This was due to an alteration in the autolytic enzymes of GISA as revealed by normal susceptibility of GISA-purified cell walls to parental strain autolysin extract and lower activity and altered peptidoglycan hydrolase activity profiles in GISA autolysin extracts compared to those of parent strains. Northern blot analysis indicated that expression of atl, the major autolysin gene, was significantly downregulated in a GISA strain compared to that of its parent strain. In contrast to whole cells, which showed decreased lysostaphin susceptibility, purified cell walls of GISA showed increased susceptibility to lysostaphin. We suggest that in our GISA strains, decreased autolytic activity is involved in the tolerance of vancomycin and the activities of endogenous autolysins are important in conferring sensitivity to lysostaphin on whole cells.


1971 ◽  
Vol 17 (7) ◽  
pp. 847-849 ◽  
Author(s):  
R. Dobardzic ◽  
P. Payment ◽  
S. Sonea

The lysogenization of Staphylococcus aureus, strain BSS, by staphylophage [Formula: see text] of serological group A may be accompanied by the loss of its capacity to synthesize δ haemolysin. The high multiplicity of infection of [Formula: see text] phage changes the tinctorial affinity of BSS cell walls and lyses the same strain lysogenic for the homologous phage; this lysis is similar to that of the staphylococcin. In negative coloration by PTA, this bacteriophage shows one elongated head (750 Å × 420 Å) and a long tail (2650 Å). Electron microscopy demonstrated also the existence of structural subunits of the tail and the hexagonal end plate. By its morphology and dimensions, the [Formula: see text] phage is similar to 594n and b594n phages studied by Bradley and to staphylophages of serological group A: 3A, 3B, 3C, 6, 7, 42E, 47, 54 of the basic set of international lysotypy.


1973 ◽  
Vol 19 (11) ◽  
pp. 1393-1399 ◽  
Author(s):  
Li-Tse Ou ◽  
A. N. Chatterjee ◽  
F. E. Young ◽  
R. E. Marquis

Cell walls isolated from a teichoic acid deficient mutant (52A5) of Staphylococcus aureus strain H were found to have lower capacities to bind cations than did walls of the parent strain. Both types of walls had higher binding affinities for Mg2+ and Ca2+ than for K+ and Na+. The reduced number of phosphate groups in 52A5 walls was reflected in a higher apparent pKa of 4.3 for displacement of Mg2+ (or Ca2+) during acid titration with HCl. The comparable pKa value for displacement of bound Mg2+ from parent-strain walls was 3.7. The reduced capacity of 52A5 walls to bind cations was not reflected in any significant increase in sensitivity to the growth inhibitory actions of ethylenediaminetetraacetate, low pH, or high NaCl concentrations. However, the 52A5 strain was somewhat more sensitive to the inhibitory effects of high pH. Also, mutant walls were found to be structurally more compact than walls of the parent strain, presumably because of less extensive electrostatic repulsion within the wall matrix.


1957 ◽  
Vol 106 (3) ◽  
pp. 365-384 ◽  
Author(s):  
Richard M. Krause

The host ranges of bacteriophages for group A, types 1, 6, 12, and 25 and group C streptococci have been determined. The findings indicate that the susceptibility to these phages is primarily a group-specific phenomenon, although it is modified by several factors such as the hyaluronic acid capsule, lysogeny, and possibly the presence of surface proteins. Phage antibody studies indicate that while the group A phages are antigenically related, they are distinct from the group C phage. This is in agreement with the observation that group A phages are not specific for their homologous streptococcal types. The purified group C carbohydrate inactivates group C phage but not the group A phages, thus suggesting that the carbohydrate, a component of the cell wall, may serve as the phage receptor site. It has not been possible to inactivate the group A phages with group A carbohydrate. Phage lysis of groups A and C streptococci is accompanied by fragmentation of the cell wall since the C carbohydrate has been identified serologically and chemically in the supernate of centrifuged lysates. The immediate lysis of groups A and C hemolytic streptococci and their isolated cell walls by an accesory heat-labile lytic factor in fresh group C lysates is also described.


2021 ◽  
Vol 8 ◽  
Author(s):  
Kristoffer T. Bæk ◽  
Camilla Jensen ◽  
Maya A. Farha ◽  
Tobias K. Nielsen ◽  
Ervin Paknejadi ◽  
...  

Staphylococcus aureus is a leading cause of bacterial infections world-wide. Staphylococcal infections are preferentially treated with β-lactam antibiotics, however, methicillin-resistant S. aureus (MRSA) strains have acquired resistance to this superior class of antibiotics. We have developed a growth-based, high-throughput screening approach that directly identifies cell wall synthesis inhibitors capable of reversing β-lactam resistance in MRSA. The screen is based on the finding that S. aureus mutants lacking the ClpX chaperone grow very poorly at 30°C unless specific steps in teichoic acid synthesis or penicillin binding protein (PBP) activity are inhibited. This property allowed us to exploit the S. aureus clpX mutant as a unique screening tool to rapidly identify biologically active compounds that target cell wall synthesis. We tested a library of ∼50,000 small chemical compounds and searched for compounds that inhibited growth of the wild type while stimulating growth of the clpX mutant. Fifty-eight compounds met these screening criteria, and preliminary tests of 10 compounds identified seven compounds that reverse β-lactam resistance of MRSA as expected for inhibitors of teichoic acid synthesis. The hit compounds are therefore promising candidates for further development as novel combination agents to restore β-lactam efficacy against MRSA.


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