The Lon protease homologue LonA, not LonC, contributes to the stress tolerance and biofilm formation of Actinobacillus pleuropneumoniae

Microbial Pathogenesis
Fang XieChunlai Wang

Abstract

Lon proteases are a family of ATP-dependent proteases that are involved in the degradation of abnormal proteins in bacteria exposed to adverse environmental stress. An analysis of the genome sequence of Actinobacillus pleuropneumoniae revealed the unusual presence of two putative ATP-dependent Lon homologues, LonA and LonC. Sequence comparisons indicated that LonA has the classical domain organization of the LonA subfamily, which includes the N-terminal domain, central ATPase (AAA) domain, and C-terminal proteolytic (P) domain. LonC belongs to the recently classified LonC subfamily, which includes Lon proteases that contain neither the N-terminal domain of LonA nor the transmembrane region that is present only in LonB subfamily members. To investigate the roles of LonA and LonC in A. pleuropneumoniae, mutants with deletions in the lonA and lonC genes were constructed. The impaired growth of the △lonA mutant exposed to low and high temperatures and osmotic and oxidative stress conditions indicates that the LonA protease is required for the stress tolerance of A. pleuropneumoniae. Furthermore, the △lonA mutant exhibited significantly reduced biofilm formation compared to the wild-type strain. However, no significant differences i...Continue Reading

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Citations

Mar 21, 2017·Applied and Environmental Microbiology·Thusitha S GunasekeraOscar N Ruiz
Nov 8, 2017·Animal Health Research Reviews·Skander HathroubiMario Jacques
Jun 27, 2020·PLoS Genetics·Avatar JoshiFitnat H Yildiz
Apr 18, 2018·Frontiers in Cellular and Infection Microbiology·Huan LiWeicheng Bei
Mar 1, 2018·Frontiers in Microbiology·Lvqin HeYiping Wen
Dec 3, 2016·The Journal of Antibiotics·Elizabeth Culp, Gerard D Wright
Jan 14, 2021·Scientific Reports·Zixing DongByong H Lee
Oct 31, 2020·Frontiers in Microbiology·Malgorzata RopelewskaIgor Konieczny
Mar 19, 2021·Saudi Journal of Biological Sciences·Madiha ZaynabShuangfei Li

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