Structural and functional properties of antimicrobial protein L5 of Lysоbacter sp. XL1

Abstract

The Gram-negative bacterium Lysobacter sp. XL1 secretes into the extracellular space five bacteriolytic enzymes that lyse the cell walls of competing microorganisms. Of special interest are homologous lytic proteases L1 and L5. This work found protein L5 to possess Gly-Gly endopeptidase and N-acetylmuramoyl-L-Ala amidase activities with respect to staphylococcal peptidoglycan. Protein L5 was found to be capable of aggregating into amyloid-like fibril structures. The crystal structure of protein L5 was determined at a 1.60-Å resolution. Protein L5 was shown to have a rather high structural identity with bacteriolytic protease L1 of Lysobacter sp. XL1 and α-lytic protease of Lysobacter enzymogenes at a rather low identity of their amino acid sequences. Still, the structure of protein L5 was revealed to have regions that differed from their equivalents in the homologs. The revealed structural distinctions in L5 are suggested to be of importance in exhibiting its unique properties.

Deletion of alpB Gene Influences Outer Membrane Vesicles Biogenesis of Lysobacter sp. XL1

“…One of the vesicle subpopulations contains bacteriolytic enzyme L5. In the process of its topogenesis, this protein accumulates in the periplasm at the inner leaflet of the OM (Kudryakova et al, 2015) in the form of amyloid-like structures (Kudryakova et al, 2018). This may lead to a pressure on the cardiolipin-enriched inner leaflet of the OM (the destabilization locus) and contribute to the formation of a subpopulation of antibacterial vesicles containing protein L5.…”

“…Notably, studies of the structural and functional features of this enzyme have revealed the formation of amyloidlike structures with increased concentration. It has been found that, in vesicles, this enzyme is namely in its amyloid-like form (Kudryakova et al, 2018). This property can be assumed to be important for initiating the formation of vesicle in the destabilization locus.…”

The First Homologous Expression System for the β-Lytic Protease of Lysobacter capsici VKM B-2533T, a Promising Antimicrobial Agent

“…Our main works investigate such enzymes in Lysobacter sp. XL1 [ 11 , 12 , 13 , 14 , 15 , 16 , 17 ]. Our recent research has been related to the study of antimicrobial potential in L. capsici VKM B-2533 T [ 6 , 10 ].…”

Влияние мутации в гене бактериолитического фермента Л5 на биогенез внешнемембранных везикул Lysobacter sp. XL1

“…XL1 [1]. С использованием методов биохимии и электронной иммуноцитохимии были получены результаты, указывающие на то, что белок Л5 принимает участие в биогенезе определённой группы секреторных везикул, содержащих его в своем составе [2][3][4]. Целью данной работы было подтвердить роль белка Л5 в этом процессе.…”