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. 1994 Jan;176(1):260–264. doi: 10.1128/jb.176.1.260-264.1994

Vancomycin-resistant Leuconostoc mesenteroides and Lactobacillus casei synthesize cytoplasmic peptidoglycan precursors that terminate in lactate.

S Handwerger 1, M J Pucci 1, K J Volk 1, J Liu 1, M S Lee 1
PMCID: PMC205040  PMID: 8282706

Abstract

The emergence of acquired high-level resistance among Enterococcus species has renewed interest in mechanisms of resistance to glycopeptide antibiotics in gram-positive bacteria. In Enterococcus faecalis and Enterococcus faecium, resistance is encoded by the van gene cluster and is due to the production of a peptidoglycan precursor terminating in D-alanyl-D-lactate, to which vancomycin does not bind. Most Leuconostoc and many Lactobacillus species are intrinsically resistant to high levels of glycopeptide antibiotics, but the mechanism of resistance has not been elucidated. To determine whether the mechanisms of resistance are similar in intrinsically resistant bacteria, cytoplasmic peptidoglycan precursors were isolated from Leuconostoc mesenteroides and Lactobacillus casei and analyzed by mass spectrometry, revealing structures consistent with UDP-N-acetylmuramyl-L-Ala-D-Glu-L-Lys-(L-Ala)-D-Ala-D-lactate and UDP-N-acetylmuramyl-L-Ala-D-Glu-L-Lys-D-Ala-D-lactate, respectively.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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