2018
DOI: 10.1017/s1466252318000142
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Mannheimia haemolyticain bovine respiratory disease: immunogens, potential immunogens, and vaccines

Abstract: Mannheimia haemolytica is the major cause of severe pneumonia in bovine respiratory disease (BRD). Early M. haemolytica bacterins were either ineffective or even enhanced disease in vaccinated cattle, which led to studies of the bacterium's virulence factors and potential immunogens to determine ways to improve vaccines. Studies have focused on the capsule, lipopolysaccharide, various adhesins, extracellular enzymes, outer membrane proteins, and leukotoxin (LKT) resulting in a strong database for understanding… Show more

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Cited by 46 publications
(31 citation statements)
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References 267 publications
(371 reference statements)
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“…M. haemolytica is a natural inhabitant of the upper respiratory tract of the bovine species, occasionally it may develop BRD outbreaks [42]. In this study, no BALF sample analyzed was positive for this bacterium.…”
Section: Discussionmentioning
confidence: 52%
“…M. haemolytica is a natural inhabitant of the upper respiratory tract of the bovine species, occasionally it may develop BRD outbreaks [42]. In this study, no BALF sample analyzed was positive for this bacterium.…”
Section: Discussionmentioning
confidence: 52%
“…F95-enrichment for deiminated proteins from serum and serum-EVs revealed a range of immunological, metabolic and gene regulatory proteins as candidates for this post-translational modification, therefore indicating hitherto under-recognized modes for protein-moonlighting of these proteins in bovine immunity and physiology. Few studies have hitherto assessed roles for PADs and deimination in cattle [22,23,42], while a range of studies have been carried out on EVs in relation to cattle immunity, fertility and development [54,57,60,61,63,65,68,74,78,83,85,88,90]. Export of post-translationally modified proteins, such as deiminated proteins in the current study, has not been assessed before in cattle serum.…”
Section: Discussionmentioning
confidence: 93%
“…They facilitate the exchange of nutrients over the outer membrane and can have important roles in pathogenesis [28,29]. M. haemolytcia ompA encodes a porin protein that has been well researched for both its role in M. haemolytica pathogenicity, and for its potential as a vaccine candidate (see [30] for review of M haemolytica OmpA). This protein has adhesive properties, as it binds to cell-surface fibronectin [31] and lactoferrin [32].…”
Section: Discussionmentioning
confidence: 99%