Specific protein-membrane interactions promote packaging of metallo- β-lactamases into outer membrane vesicles

We report that favorable electrostatic protein-membrane interactions are also at work in the soluble enzyme IMP-1, while being absent in VIM-2. These interactions correlate with an enhanced incorporation of IMP-1 compared to VIM-2 into OMVs. Disruption of these interactions in NDM-1 and IMP-1 impairs their inclusion into vesicles, confirming their role in defining the protein cargo in OMVs. These results also indicate that packaging of metallo-β-lactamases into vesicles in their active form is a common phenomenon that involves cargo selection based on specific molecular interactions.PMID:34310214 | DOI:10.1128/AAC.00507-21

Source: Antimicrobial Agents and Chemotherapy - July 26, 2021 Category: Microbiology Authors: Carolina L ópez Alessio Prunotto Guillermo Bahr Robert A Bonomo Lisandro J Gonz ález Matteo Dal Peraro Alejandro J Vila Source Type: research