The Chemical Basis for the Action of the Vancomycin Group of Antibiotics

Perkins, H. R.; Nieto, Manuel

doi:10.1111/j.1749-6632.1974.tb43276.x

Cited by 90 publications

(64 citation statements)

References 32 publications

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“…As shown in Table 1, mutant strain Sep1 was 5 to 10 times more susceptible than the GBS parental strain to all ␤-lactam antibiotics tested. However, the two strains differed only slightly in sensitivity to vancomycin, known to complex with the D-alanyl-D-alanine subunits of the peptidoglycan polymer (38). Strikingly, the GBS parent and the Sep1 mutant differed significantly in susceptibility to different classes of antibiotics known to act intracellularly.…”

Section: Vol 183 2001 Identification and Molecular Analysis Of Pcsbmentioning

confidence: 91%

Identification and Molecular Analysis of PcsB, a Protein Required for Cell Wall Separation of Group B Streptococcus

et al. 2001

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Group B streptococcus (GBS) is the leading cause of bacterial sepsis and meningitis in neonates. N-terminal sequencing of major proteins in the culture supernatant of a clinical isolate of GBS identified a protein of about 50 kDa which could be detected in all of 27 clinical isolates tested. The corresponding gene, designated pcsB, was isolated from a GBS cosmid library and subsequently sequenced. The deduced PcsB polypeptide consists of 447 amino acid residues (M r , 46,754), carries a potential N-terminal signal peptide sequence of 25 amino acids, and shows significant similarity to open reading frames of unknown function from different organisms and to the murein hydrolase P45 from Listeria monocytogenes. Northern blot analysis revealed a monocistronic transcriptional organization for pcsB in GBS. Insertional inactivation of pcsB in the genome of GBS resulted in mutant strain Sep1 exhibiting a drastically reduced growth rate compared to the parental GBS strain and showing an increased susceptibility to osmotic pressure and to various antibiotics. Electron microscopic analysis of GBS mutant Sep1 revealed growth in clumps, cell separation in several planes, and multiple division septa within single cells. These data suggest a pivotal role of PcsB for cell division and antibiotic tolerance of GBS.Group B streptococcus (GBS), also known as Streptococcus agalactiae, is part of the normal human flora colonizing the respiratory, gastrointestinal, and urogenital tracts. It is also the leading cause of bacterial sepsis and meningitis in neonates in the United States and western Europe, and it is a major cause of endocarditis and fever in parturient women (2). In the last decade, the incidence of GBS infections has increased especially in the elderly and in immunocompromised persons (58), but despite its clinical importance, GBS is only poorly understood on the molecular level.Bacterial cell division is a complex interplay of topological processes, biosynthetic reactions, and cleavage mechanisms. Septum formation is initiated by the cooperative action of division inhibitors, topological specificity factors, and proteins constituting the cell division apparatus both found in gramnegative and gram-positive bacteria (reviewed in reference 5, 31, and 42). In globular cells, like streptococci, the division septum can be arranged in several orientations, resulting in the generation of two daughter cells of the same size and shape. The choice of the division plane determines the three-dimensional organization of the multicellular arrays of progeny cells that are formed. In GBS, the plane of division is approximately the same in each division cycle, resulting in the formation of frequently long chains (20). The division septum that is formed between the daughter cells is composed of newly synthesized membrane and peptidoglycan components. Peptidoglycan biosynthesis is accomplished by the insertion of peptide-carrying disaccharide units into the existing murein sacculus by transglycosylation and transpeptidation (34). Cell divi...

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Section: Vol 183 2001 Identification and Molecular Analysis Of Pcsbmentioning

confidence: 91%

Identification and Molecular Analysis of PcsB, a Protein Required for Cell Wall Separation of Group B Streptococcus

et al. 2001

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“…A very small peak (_1%) was present in a position slightly more cathodal than the largest peak. Vancomycin (16) and a mol wt of 2,000 (17).…”

Section: Methodsmentioning

confidence: 99%

The Effects of Ristocetin and von Willebrand Factor on Platelet Electrophoretic Mobility

Coller¹

1978

J. Clin. Invest.

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“…Studies on the association of vancomycin with various peptides have indicated features of the peptide that facilitate complex formation (15,16,(18)(19)(20). Since certain analogues of UDP-MurNAc-pentapeptide are utilized for peptidoglycan synthesis (7), it was of interest to compare the sensitivity of the system to vancomycin with different substrates.…”

Section: Materials and Menrhodsmentioning

confidence: 99%

“…The mechanism of action of this antibiotic appears to be related to its ability to complex with the D-alanyl-D-alanine moieties that are present in various phases of polymer synthesis (18)(19)(20). It has not been established unequivocally in which phase the primary site of action is located.…”

mentioning

confidence: 99%

On the Mechanism of Action of Vancomycin: Inhibition of Peptidoglycan Synthesis in Gaffkya homari

Hammes

Neuhaus

1974

Antimicrob Agents Chemother

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The Chemical Basis for the Action of the Vancomycin Group of Antibiotics

Cited by 90 publications

References 32 publications

Identification and Molecular Analysis of PcsB, a Protein Required for Cell Wall Separation of Group B Streptococcus

Identification and Molecular Analysis of PcsB, a Protein Required for Cell Wall Separation of Group B Streptococcus

The Effects of Ristocetin and von Willebrand Factor on Platelet Electrophoretic Mobility

On the Mechanism of Action of Vancomycin: Inhibition of Peptidoglycan Synthesis in Gaffkya homari

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