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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.   Electronic supplementary material  The online version of this article (doi:10.1186/s13567-016-0378-1) contains supplementary material, which is available to authorized users.

Two outer membrane proteins are bovine lactoferrin-binding proteins in Mannheimia haemolytica A1