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Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1
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Journal Article
Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1
2016
Overview
Mannheimia haemolytica
is a Gram negative bacterium that is part of the bovine respiratory disease, which causes important economic losses in the livestock industry. In the present work, the interaction between
M. haemolytica
A1 and bovine lactoferrin (BLf) was studied. This iron-chelating glycoprotein is part of the mammalian innate-immune system and is present in milk and mucosal secretions; Lf is also contained in neutrophils secondary granules, which release this glycoprotein at infection sites. It was evidenced that
M. haemolytica
was not able to use iron-charged BLf (BholoLf) as a sole iron source; nevertheless, iron-lacked BLf (BapoLf) showed a bactericidal effect against
M. haemolytica
with MIC of 4.88 ± 1.88 and 7.31 ± 1.62 μM for
M. haemolytica
strain F (field isolate) and
M. haemolytica
strain R (reference strain), respectively. Through overlay assays and 2-D electrophoresis, two OMP of 32.9 and 34.2 kDa with estimated IP of 8.18 and 9.35, respectively, were observed to bind both BapoLf and BholoLf; these OMP were identified by Maldi-Tof as OmpA (heat-modifiable OMP) and a membrane protein (porin). These
M. haemolytica
BLf binding proteins could be interacting in vivo with both forms of BLf depending on the iron state of the bovine.
Publisher
BioMed Central,BioMed Central Ltd,Springer Nature B.V
Subject
/ Animals
/ bacteria
/ Bacterial Outer Membrane Proteins - immunology
/ Bacterial Outer Membrane Proteins - metabolism
/ Cattle
/ Electrophoresis, Gel, Two-Dimensional
/ granules
/ Mannheimia haemolytica - immunology
/ Mannheimia haemolytica - metabolism
/ Medicine
/ milk
/ Molecular Docking Simulation
/ Pasteurellosis, Pneumonic - immunology
/ Pasteurellosis, Pneumonic - metabolism
/ porins
/ Veterinary Medicine/Veterinary Science
/ Virology
