LdtMav2, a nonclassical transpeptidase and susceptibility of Mycobacterium avium to carbapenems.
AIM
Mycobacterium avium infections, especially in immune-compromised individuals, present a significant challenge as therapeutic options are limited. In this study, we investigated if M. avium genome encodes nonclassical transpeptidases and if newer carbapenems are effective against this mycobacteria.


MATERIALS & METHODS
Biochemical and microbiological approaches were used to identify and characterize a nonclassical transpeptidase, namely L,D-transpeptidase, in M. avium.


RESULTS & CONCLUSION
We describe the biochemical and physiological attributes of a L,D-transpeptidase in M. avium, LdtMav2. Suggestive of a constitutive requirement, levels of LdtMav2, a L,D-transpeptidase in M. avium, remain constant during exponential and stationary phases of growth. Among β-lactam antibacterials, only a subset of carbapenems inhibit LdtMav2 and tebipenem, a new oral carbapenem, inhibits growth of M. avium.
['Mattoo|Rohini|R|', 'Lloyd|Evan P|EP|', 'Kaushik|Amit|A|', 'Kumar|Pankaj|P|', 'Brunelle|Julie L|JL|', 'Townsend|Craig A|CA|', 'Lamichhane|Gyanu|G|']
D000900:Anti-Bacterial Agents D015780:Carbapenems D018360:Crystallography, X-Ray D024901:Drug Resistance, Multiple, Bacterial D016680:Genome, Bacterial D015269:Mycobacterium avium Complex D010458:Peptidyl Transferases D017422:Sequence Analysis, DNA D047090:beta-Lactams
Mycobacterium avium carbapenem mycobacteria L,D-transpeptidase tebipenem peptidoglycan