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Biomedical subjects

M R Smith

Publications and source records attributed to M R Smith.

At least 253 records · Page 14Linked to original sources
PubMed1971

Induction of hemolysin synthesis by tranformation in Staphylococcus aureus.

A nonhemolytic strain of Staphylococcus aureus was transformed with deoxyribonucleic acid extracted from two hemolytic strains of S. aureus. In each case the hemolysin pattern after transformation was identical to that of the donor strain. However, bacteriophage type, serotypes, and other biological properties of the recipient strain remained unaffected.

Bacteriological Techniques↗
PubMed1970

Biological and Immunological Properties of Encapsulated Strains of Staphylococcus aureus from Human Sources.

Of 875 strains of Staphylococcus aureus isolated from human source clinical specimens, 37 (4.2%) were encapsulated strains. These were all negative for clumping factor and could not be typed with bacteriophages or by serology. Twenty-one of these did not produce any hemolysins, 15 produced alpha hemolysin, 1 produced beta hemolysin, and 1 produced both beta and delta hemolysins. After one or two subcultures, 27 of the encapsulated strains converted to the compact variant form, all became positive for clumping factor, 12 became phage-typable, and 24 became sero-typable. In addition, 7 strains converted from negative to alpha hemolysin production. Comparison of phage- and sero-types did not reveal any relationships. Immunologically, mice challenged with heat-killed encapsulated strains were protected against a challenge infection with the Smith diffuse strain. Protective antibodies in rabbit anti-Smith diffuse strain antisera were removed by adsorption using the encapsulated organisms isolated in this study. The adsorbed sera no longer protected against challenge infection in mice with the Smith diffuse strain. From these results, it appears that the encapsulated strains isolated were immunologically and biologically similar to the classical Smith diffuse strain.

Journal Article↗
PubMed1970

Cholesterol inhibition of isopentenyl pyrophosphate delta3, delta2-isomerase in Mycoplasma laidlawii.

Cholesterol inhibits isopentenyl Delta(3),Delta(2)-isomerase of Mycoplasma laidlawii in an apparently competitive fashion. The conversion of mevalonic acid to isopentenyl pyrophosphate is slightly stimulated. Organisms grown in the presence of mevalonic-2-(14)C acid contain small amounts of radio-label in nucleic acid and protein fractions. Most of the label is found in the lipids and is reduced dramatically in organisms grown with cholesterol. No significant accumulation of phosphorylated intermediates of polyterpene biosynthesis was observed in cells or culture supernatant fluid. All of the radioactivity appearing in the nucleic acid fraction occurs in the minor nucleoside, isopentenyl adenosine, of the transfer ribonucleic acid. The necessity for synthesis by the organisms of this minor nucleoside from mevalonic acid may explain the site of enzyme inhibition by cholesterol of polyterpene biosynthesis.

Carbon Isotopes↗
PubMed1969

Heat labile opsonins to pneumococcus. I. Participation of complement.

Heat labile opsonins (HLO) in normal rat serum to both encapsulated and unencapsulated pneumococci (a) have the same heat lability as complement (C); (b) are active at 37 degrees C but not at 0 degrees C; (c) are inactivated proportionately to hemolytic C by the addition of immune aggregates to the serum; (d) are adsorbed from serum nonspecifically by bacteria at 37 degrees C but not at 0 degrees C; (e) are Ca(++)- and/or Mg(++)-dependent in their action; and (f) are inactivated by zymosan and a purified cobra venom factor, and in the case of encapsulated pneumococci, at least, by NH(4)OH. Like other opsonins, HLO to pneumococci act primarily on the bacteria rather than on the phagocytes. Their combined properties indicate that they involve multiple components of the hemolytic C system. Since HLO are immunologically polyspecific, they presumably play a broad protective role in the early (preantibody) phase of acute bacterial infections.

Adsorption↗
PubMed1969

Heat labile opsonins to pneumococcus. II. Involvement of C3 and C5.

When encapsulated type 25 pneumococci (Pn25) were opsonized with normal guinea pig serum, they consumed much more C3 than other complement (C) components. Fixation of C3 to the organisms was demonstrated by radio-labeling techniques, and its capsular localization was established by the use of monospecific anti-C3 antibody. Treatment of the serum with an appropriate dose of a purified cobra venom factor (VF) destroyed C3 and all of the opsonic activity, without appreciably affecting the other C components. Addition of purified C3 completely restored the opsonic activity of the VF-treated serum, indicating a requirement for C3. Since purified C3 alone had no opsonic activity, it was concluded that the C3 molecules had to be cleaved (to C3b) to function as opsonins. Experiments with C5-deficient mice revealed that C5 also plays a definite, but quantitatively less impressive, role in antipneumococcal defense.

Animals↗
PubMed1969

Natural immunity to bacterial infections: the relation of complement to heat-labile opsonins.

Heat-labile opsonins to pneumococci in normal mammalian sera, unlike antibodies, fail to interact with the bacteria at 0 degrees C and require Ca(++) and/or Mg(++). They are readily removed from serum by antigen-antibody complexes that fix complement (C) and are inhibited by reagents that inactivate various C components. The principal heat-labile opsonin to pneumococci is activated C3 (C3(b)), but a slight enhancing effect is exerted by one or more of the late-reacting components of the hemolytic complement system (C5-C9). Since heat-labile opsonins are immunologically polyspecific, they presumably play a broad protective role in the early (preantibody) phase of acute bacterial infections.

Animals↗