Dataset Information

Proteomic Analysis of Outer Membrane Vesicles Derived from the Type A5 Strain of Mannheimia haemolytica

ABSTRACT: Mannheimia haemolytica (M. haemolytica) cause mastitis in sheep, acute sepsis in newborn lambs, and co-infections with various pathogens, leading to bovine respiratory disease syndrome (BRDS), these infections have resulted in significant economic losses to both domestic and international farming industries. An in-depth understanding of the pathogenic mechanisms of M. haemolytica is crucial for the prevention and control of this disease. Outer membrane vesicles (OMVs) play a vital role in bacterial pathogenesis, serving as key mediators of interactions between Gram-negative bacteria and their hosts. However, the specific role of OMVs in the pathogenic process of M. haemolytica remains poorly understood. To address this, we isolated OMVs from the Mannheimia haemolytica Type A5 strain (MH-5) using ultracentrifugation and subsequently characterized their secretory properties, protein composition, and immunogenicity through electron microscopy, liquid chromatography-tandem mass spectrometry (LC-MS/MS), and cellular experiments. The electron microscopy results indicated that the MH-5 strain secreted OMVs under natural growth conditions. Proteomic and bioinformatics analyses revealed that these OMVs contained 282 proteins, with significant enrichment in proteins related to immunity, iron metabolism, and catalytic activity. Cellular experiments demonstrated that, compared to the control group, the OMVs group exhibited a significant increase in the mRNA expression of IL-1β, IL-6, and TNF-α, with secretion levels increasing in a dose-dependent manner, thereby enhancing the inflammatory response. These findings lay the groundwork for further exploration of the role of OMVs in the pathogenesis of M. haemolytica and provide insights for the development of effective vaccines and antibiotics against this pathogen.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mannheimia Haemolytica M42548

TISSUE(S): Germ

SUBMITTER: YuanJi Gao

LAB HEAD: Gao Yuanji

PROVIDER: PXD064633 | Pride | 2025-06-30

REPOSITORIES: Pride

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			Action	DRS
	MH_20240111182422.raw	Raw
	MH_20240111182422.xlsx	Xlsx
	checksum.txt	Txt

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Publications

Proteomic analysis of outer membrane vesicles derived from the type A5 Strain of Mannheimia haemolytica.

Shang Ke K Gao Yuanji Y Du Jiangbo J Liu Chang C Dai Jinglei J Zhang Junfeng J Jia Yanyan Y Yu Zuhua Z Chen Songbiao S Liu Zhongyu Z

Frontiers in cellular and infection microbiology 20250611

Mannheimia haemolytica (M. haemolytica) cause mastitis in sheep, acute sepsis in newborn lambs, and co-infections with various pathogens, leading to bovine respiratory disease syndrome (BRDS), these infections have resulted in significant economic losses to both domestic and international farming industries. An in-depth understanding of the pathogenic mechanisms of M. haemolytica is crucial for the prevention and control of this disease. Outer membrane vesicles (OMVs) play a ...[more]

PMID: 40568700

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Project description:Tenacibaculum maritimum, the etiological agent of tenacibaculosis in marine fish, constitutively secretes extracellular products (ECPs), which play a main role in virulence. However, their protein content has not been yet comprehensively studied. In this study a collection of 64 T. maritimum strains belonging to the four serotypes described so far (O1 to O4) was used to analyse the prevalence of extracellular proteolytic and lipolytic activities related to virulence. Results showed the existence of a large heterogeneity of the enzymatic capacity among serotype O4 isolates. Most notably, the ECPs of T. maritimum SP9.1 belonging to serotype O4 contain a large amount of outer membrane vesicles (OMVs), which were characterized by electron microscopy and purified by successive steps of filtration and centrifugation. Total protein content of ECPs, and the proteins associated to OMVs and soluble fraction of the ECPs (S-ECPs) were identified by nLC-TIMS-QTOF. A total of 641 proteins were identified in ECPs including some virulence related factors, which were mainly found in one of the fractions, either in OMVs or S-ECPs. Outer membrane proteins such as TonB-dependent transporters and the T9SS-related proteins PorP, PorT and SprA appeared to be mainly associated with OMVs. By contrast, putative virulence factors such as sialidase SiaA, chondroitinase CslA, sphingomyelinase Sph, ceramidase Cer and collagenase Col were found only in the S-ECPs. These findings demonstrate that T. maritimum release, through surface blebbing, outer membrane vesicles that are enriched specifically in TonB-dependent siderophore transporters and proteins of the type IX secretion system. Interestingly, our results also showed that OMVs could play a role in virulence by promoting surface adhesion, biofilm formation, and maximizing cytotoxic effects of the ECPs. The T. maritimum secretome analysis provides insights into the extracellular products function and can constitute the basis for future studies aimed to elucidate the role of OMVs in the pathogenesis of fish tenacibaculosis.

Dataset Information

Proteomic Analysis of Outer Membrane Vesicles Derived from the Type A5 Strain of Mannheimia haemolytica

Dataset's files

Publications

Proteomic analysis of outer membrane vesicles derived from the type A5 Strain of <i>Mannheimia haemolytica</i>.

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OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Proteomic Analysis of Outer Membrane Vesicles Derived from the Type A5 Strain of Mannheimia haemolytica

Dataset's files

Publications

Proteomic analysis of outer membrane vesicles derived from the type A5 Strain of &lt;i&gt;Mannheimia haemolytica&lt;/i&gt;.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Proteomic analysis of outer membrane vesicles derived from the type A5 Strain of <i>Mannheimia haemolytica</i>.