Abstract

Listeria monocytogenes' peptidoglycan�¢â�¬â�¢s meso-diaminopimelic acid residues are amidated by AsnB, which also has an impact on the bacterial surface characteristics and host cell invasion.

Author(s): Joe Wilson

It was discovered that a Listeria monocytogenes ScottA mutant with a transposon in the asnB gene's 5' untranslated region was extremely sensitive to the antibiotic t-cinnamaldehyde. Here, we describe the functional characterization of AsnB in intracellular infection and peptidoglycan (PG) modification. Although sequence alignment revealed that AsnB of Listeria is closely linked to a collection of homologs that catalyse the amidation of meso-diaminopimelic acid (mDAP) residues in the peptidoglycan of other bacterial species, this protein is designated as a glutamine-dependent asparagine synthase. According to a structural study of the peptidoglycan from an asnB mutant compared to isogenic wild-type (WT) and complemented mutant strains, asnB mediates mDAP amidation in L. monocytogenes. Numerous peptidoglycan and cell surface-related abnormalities were brought on by mDAP amidation deficiency in asnB. It was discovered that a Listeria monocytogenes ScottA mutant with a transposon in the asnB gene's 5' untranslated region was extremely sensitive to the antibiotic t-cinnamaldehyde. Here, we describe the functional characterization of AsnB in intracellular infection and peptidoglycan (PG) modification. Although sequence alignment revealed that AsnB of Listeria is closely linked to a collection of homologs that catalyse the amidation of meso-diaminopimelic acid (mDAP) residues in the peptidoglycan of other bacterial species, this protein is designated as a glutamine-dependent asparagine synthase. According to a structural study of the peptidoglycan from an asnB mutant compared to isogenic wild-type (WT) and complemented mutant strains, asnB mediates mDAP amidation in L. monocytogenes. Numerous peptidoglycan and cell surface-related abnormalities in asnB, bacterial virulence, and InlA were caused by mDAP amidation deficiency