Crystal Structure of VapBC-1 from Nontypeable Haemophilus influenzae and the Effect of PIN Domain Mutations on Survival during Infection

• DOI: 10.1128/jb.00026-19
• Publication Date: 2019-04-02T11:50:57Z
• Authors: Ashley L. Molinaro; Maithri M. Kaship...; Scott Lovell; Kevin P. Battaile; Nathan P. Coussens; Min Shen; Dayle A. Daines
• Keywords: Antitoxin; Wild type

Herein the crystal structure of VapBC-1 complex from nontypeable Haemophilus influenzae (NTHi) is described. Our results show that some mutations in PIN domain VapC-1 toxin were associated with decreased toxicity E. coli , but mutants retained ability to homodimerize and heterodimerize wild-type cognate antitoxin, VapB-1. A new system was designed constructed quantify effects these on NTHi survival during infections primary human tissues ex vivo . Any mutation a conserved amino acid significantly number survivors compared cis under same conditions.