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PubMed1973

Polysaccharides of the genus Bacillus cross-reactive with the capsular polysaccharides of Diplococcus pneumoniae type 3, Haemophilus influenzae type b, and Neisseria meningitidis group A.

We studied 174 strains of the genus Bacillus for cross-reacting antigens to the capsular polysaccharides of groups A and C meningococcus, types I and III pneumococcus, and Haemophilus influenzae type b. Cross-reactions were detected by immunodiffusion in agarose gel by using type-specific antisera and confirmed by absorption and inhibition experiments. Of 20 Bacillus pumilis strains, six had an antigen cross-reacting with group A meningococcal polysaccharide. Other cross-reactions included one strain of B. pumilis with H. influenzae type b, one of B. cereus var. mycoides with pneumococcus type III, and one of B. alvei with both type b and SIII polysaccharides. These cross-reacting antigens are polysaccharides of vegetative cells and may be extracellular in location. Because these bacilli have antigens cross-reacting with the virulence factors of pyogenic bacteria, they may, as normal flora, be an antigenic stimulus for "natural" serum anti-capsular antibodies to the type b Haemophilus and group A meningococcus polysaccharides.

Antigens, Bacterial↗
PubMed1973

Adenosine triphosphate-dependent deoxyribonuclease from Diplococcus pneumoniae: fate of transforming deoxyribonucleic acid in a strain deficient in the enzymatic activity.

The adenosine triphosphate-dependent deoxyribonuclease is required for wild-type levels of deoxyribonucleic acid (DNA) repair and genetic recombination. In an attempt to determine the physiological function of this enzyme in pneumococcal transformation, the fate of transforming DNA was followed in a wild-type strain and in a strain lacking the enzymatic activity. The qualitative and quantitative findings were closely comparable in the two strains through the step of physical association of a single strand of donor DNA with the recipient chromosome. These results are interpreted to mean that the enzyme may be involved in the subsequent hypothetical removal of excess polynucleotide sequences during conversion of the presumed hydrogen-bonded intermediate into a covalently linked recombinant structure.

Adenosine Triphosphate↗