Structural highlights
Function
ELAS_PSEAB Cleaves host elastase, collagen, IgI and several complement components as well as endogenous pro-aminopeptidase, pro-chitin-binding protein (cbpD). Cleaves its own pro-peptide. Involved in the pathogenesis of P.aeruginosa infections.[UniProtKB:P14756]
Publication Abstract from PubMed
The human pathogen Pseudomonas aeruginosa has a number of virulence factors at its disposal that play crucial roles in the progression of infection. LasB is one of the major virulence factors and exerts its effects through elastolytic and proteolytic activities aimed at dissolving connective tissue and inactivating host defense proteins. LasB is of great interest for the development of novel patho-blockers to temper the virulence, but access has thus far largely been limited to protein isolated from Pseudomonas cultures. Here, we describe a new protocol for high-level production of native LasB in E. coli. We demonstrate that this facile approach is suitable for the production of mutant, thus far inaccessible LasB variants, and characterize the proteins biochemically and structurally. We expect that easy access to LasB is going to accelerate the development of inhibitors for this important virulence factor.
Facile Production of the Pseudomonas aeruginosa Virulence Factor LasB in E. coli for Structure-Based Drug Design.,Kolling D, Haupenthal J, Hirsch AKH, Kohnke J Chembiochem. 2023 May 17:e202300185. doi: 10.1002/cbic.202300185. PMID:37195753[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kolling D, Haupenthal J, Hirsch AKH, Köhnke J. Facile Production of the Pseudomonas aeruginosa Virulence Factor LasB in E. coli for Structure-Based Drug Design. Chembiochem. 2023 May 17:e202300185. PMID:37195753 doi:10.1002/cbic.202300185
