scholarly journals Differences between predicted outer membrane proteins of genotype 1 and 2 Mannheimia haemolytica

2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Michael L. Clawson ◽  
Gennie Schuller ◽  
Aaron M. Dickey ◽  
James L. Bono ◽  
Robert W. Murray ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Mannheimia Haemolytica ◽  
Genotype 1

scholarly journals Differences between Predicted Outer Membrane Proteins of Pasteurella multocida, Histophilus somni, and Genotype 1 and 2 Mannheimia haemolytica Strains Isolated from Cattle

Genome ◽  
2021 ◽  
Author(s):  
Emily L Wynn ◽  
Michael Clawson
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Pasteurella Multocida ◽  
Outer Membrane Proteins ◽  
Host Immunity ◽  
Mannheimia Haemolytica ◽  
Genotype 1 ◽  
The Core ◽  
Histophilus Somni ◽  
Genotype 2

Common bacterial causes of bovine respiratory disease (BRD) include Histophilus somni, Mannheimia haemolytica, and Pasteurella multocida. Within M. haemolytica, two major genotypes are commonly found in cattle (1 and 2), however, genotype 2 strains are isolated from diseased lungs much more frequently than genotype 1 strains. Outer membrane proteins (OMPs) of H. somni, P. multocida, and genotype 2 M. haemolytica may be important factors for acquired host immunity. Predicted OMP differences between genotype 1 and 2 M. haemolytica have been previously identified. In this study, we expanded that focus to include bovine-isolated strain genomes representing all three species and the two M. haemolytica genotypes. Reported here are the core genomes unique to each of them, core genomes shared between some or all combinations of the three species and two M. haemolytica genotypes, and predicted OMPs within these core genomes. The OMPs identified in this study are potential candidates for further study and the development of interventions against BRD.

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

2016 ◽  
Vol 47 (1) ◽  
Author(s):  
Luisa Samaniego-Barrón ◽  
Sarahí Luna-Castro ◽  
Carolina Piña-Vázquez ◽  
Francisco Suárez-Güemes ◽  
Mireya de la Garza
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Binding Proteins ◽  
Outer Membrane Proteins ◽  
Mannheimia Haemolytica ◽  
Bovine Lactoferrin

scholarly journals Immunogenicity of Mannheimia haemolytica Recombinant Outer Membrane Proteins Serotype 1-Specific Antigen, OmpA, OmpP2, and OmpD15

2011 ◽  
Vol 18 (12) ◽  
pp. 2067-2074 ◽  
Author(s):  
Sahlu Ayalew ◽  
Binu Shrestha ◽  
Marie Montelongo ◽  
Amanda E. Wilson ◽  
Anthony W. Confer
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Recombinant Proteins ◽  
Outer Membrane Proteins ◽  
Specific Antigen ◽  
Antibody Responses ◽  
Mannheimia Haemolytica ◽  
Content Type ◽  
Outer Membranes ◽  
Serotype 1

ABSTRACTWe previously identifiedMannheimia haemolyticaouter membrane proteins (OMPs) that may be important immunogens by using immunoproteomic analyses. Genes for serotype 1-specific antigen (SSA-1), OmpA, OmpP2, and OmpD15 were cloned and expressed, and recombinant proteins were purified. Objective 1 of this study was to demonstrate immunogenicity of the four recombinant OMPs in mice and cattle. Objective 2 was to determine if the addition of individual recombinant OMPs or combinations of them would modify immune responsiveness of mice to the recombinant chimeric protein SAC89, containing the main epitope fromM. haemolyticaouter membrane lipoprotein PlpE and the neutralizing epitope ofM. haemolyticaleukotoxin. Mice vaccinated with recombinant OmpA (rOmpA), rSSA-1, rOmpD15, and rOmpP2 developed significant antibody responses toM. haemolyticaouter membranes and to the homologous recombinant OMP. Cattle vaccinated with rOmpA and rSSA-1 developed significant antibodies toM. haemolyticaouter membranes by day 28, whereas cattle vaccinated with rOmpD15 and rOmpP2 developed only minimal responses. Sera from cattle vaccinated with each of the recombinant proteins stimulated complement-mediated killing of the bacterium. Concurrent vaccination with SAC89 plus any of the four rOMPs singly resulted in increased endpoint anti-SAC89 titers, and for the SAC89/rSSA-1 vaccinees, the response was increased significantly. In contrast, the SAC89/P2/SSA-1 and SAC89/OmpA/P2/D15/SSA-1 combination vaccines resulted in significant decreases in anti-SAC89 antibodies compared to SAC89 vaccination alone. In conclusion, under the conditions of these experiments, vaccination of mice and cattle with rOmpA and rSSA-1 stimulated high antibody responses and may have protective vaccine potential.

scholarly journals The Conservation of Low Complexity Regions in Bacterial Proteins Depends on the Pathogenicity of the Strain and Subcellular Location of the Protein

Genes ◽  
2021 ◽  
Vol 12 (3) ◽  
pp. 451
Author(s):  
Pablo Mier ◽  
Miguel A. Andrade-Navarro
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Bacterial Species ◽  
Outer Membrane Proteins ◽  
Subcellular Location ◽  
Low Complexity ◽  
Extracellular Proteins ◽  
Bacterial Strains ◽  
Bacterial Proteins ◽  
Protein Subcellular Location

Low complexity regions (LCRs) in proteins are characterized by amino acid frequencies that differ from the average. These regions evolve faster and tend to be less conserved between homologs than globular domains. They are not common in bacteria, as compared to their prevalence in eukaryotes. Studying their conservation could help provide hypotheses about their function. To obtain the appropriate evolutionary focus for this rapidly evolving feature, here we study the conservation of LCRs in bacterial strains and compare their high variability to the closeness of the strains. For this, we selected 20 taxonomically diverse bacterial species and obtained the completely sequenced proteomes of two strains per species. We calculated all orthologous pairs for each of the 20 strain pairs. Per orthologous pair, we computed the conservation of two types of LCRs: compositionally biased regions (CBRs) and homorepeats (polyX). Our results show that, in bacteria, Q-rich CBRs are the most conserved, while A-rich CBRs and polyA are the most variable. LCRs have generally higher conservation when comparing pathogenic strains. However, this result depends on protein subcellular location: LCRs accumulate in extracellular and outer membrane proteins, with conservation increased in the extracellular proteins of pathogens, and decreased for polyX in the outer membrane proteins of pathogens. We conclude that these dependencies support the functional importance of LCRs in host–pathogen interactions.

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