Uncovering the structure and function of Pseudomonas aeruginosa periplasmic proteins by an in silico approach. Issue 15 (12th October 2020)

• Record Type: Journal Article
• Authors: Caprari, Silvia; Brandi, Valentina; Pasquadibisceglie, Andrea; Polticelli, Fabio
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 38:Issue 15(2020)
• Page Start: 4508
• Page End: 4520
• Publication Date: 2020-10-12
• Subjects: Pseudomonas aeruginosa -- periplasmic proteins -- molecular modeling -- protein function recognition -- drug targets; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2019.1683468
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract: Pseudomonas aeruginosa is an opportunistic human pathogen highly relevant from a biomedical viewpoint. It is one of the main causes of infection in hospitalized patients and a major cause of mortality of cystic fibrosis patients. This is also due to its ability to develop resistance to antibiotics by various mechanisms. Therefore, it is urgent and desirable to identify novel targets for the development of new antibacterial drugs against Pseudomonas aeruginosa . In this work this problem was tackled by an in silico approach aimed at providing a reliable structural model and functional annotation for the Pseudomonas aeruginosa periplasmic proteins for which these data are not available yet. A total of 83 protein sequences were analyzed, and the corresponding structural models were built, leading to the identification of 32 periplasmic 'substrate-binding proteins', 14 enzymes and 4 proteins with different functions, including lipids and metals binding. The most interesting cases were found within the 'enzymes' group with the identification of a lipase, which can be regarded as a virulence factor, a protease involved in the assembly of β-barrel membrane proteins and a l, d -transpeptidase, which could contribute to confer resistance to β-lactam antibiotics to the bacterium. Communicated by Ramaswamy H. Sarma