Muropeptide modification-amidation of peptidoglycan D-glutamate does not affect the proinflammatory activity of Staphylococcus aureus.
Peptidoglycan muropeptides, potent proinflammatory components, are amidated in Staphylococcus aureus for unknown reasons. To study whether this modification may modulate proinflammatory capacity, cytokine induction by isogenic S. aureus strains with different amidation levels and by synthetic amidated/nonamidated muramyldipeptides was evaluated. However, amidation did not significantly affect cytokine induction. This finding contributes to defining peptidoglycan receptor specificities and indicates that further rationales for muropeptide amidation have to be considered.
Kraus
Dirk
D
Medical Microbiology and Hygiene Institute, University of Tübingen, Elfriede-Aulhorn-Strasse 6, 72076 Tübingen, Germany.
Kalbacher
Hubert
H
Buschmann
Julia
J
Berger-Bächi
Brigitte
B
Götz
Friedrich
F
Peschel
Andreas
A
D000119:Acetylmuramyl-Alanyl-Isoglutamine / Q000138:chemical synthesis / Q000737:chemistry / Q000276:immunology*; D016207:Cytokines / Q000096:biosynthesis; D017353:Gene Deletion; D018698:Glutamic Acid / Q000378:metabolism*; D006801:Humans; D007963:Leukocytes, Mononuclear / Q000276:immunology / Q000382:microbiology; D010457:Peptidoglycan / Q000737:chemistry* / Q000276:immunology*; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000276:immunology*
D016207:Cytokines; D010457:Peptidoglycan; D018698:Glutamic Acid; D000119:Acetylmuramyl-Alanyl-Isoglutamine