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Protein composition of the biofilm matrix and the outer membrane vesicles (OMVs) during iron-sufficient and iron-restricted growth.

ABSTRACT: There is limited efficacy in vaccines currently available to prevent some animal diseases of bacterial origin, such as bovine respiratory disease due to Histophilus somni. Protective efficacy can potentially be improved if bacterial antigens expressed in the host are included in vaccines. During H. somni infection in the bovine host, biofilms become established and the availability of essential iron is restricted. To investigate potential proteins as protective antigens, the protein composition of spontaneously released outer membrane vesicles (OMVs) during iron-sufficient and iron-restricted growth, and the proteins expressed in the biofilm matrix were analyzed and compared. Proteomic analysis revealed a dramatic physiological change in H. somni as it transitioned from the planktonic form to the biofilm mode of growth. All transferrin-binding proteins (Tbp) previously identified in H. somni were detected in the OMVs, suggesting that OMVs could induce antibodies to these proteins. Two TbpA-like proteins and 7 total proteins were present in the OMVs only when iron was restricted, indicating that the expression of these Tbp was differentially regulated. More proteins associated with quorum-sensing (QS) signaling were detected in the biofilm matrix compared with proteins in the OMVs, supporting a link between QS and biofilm formation. Proteins ACA31267.1 (OmpA) and ACA32419.1 (TonB-dependent receptor) were present in the OMV and biofilm matrix, and predicted to be potential protective antigens using an immuno-bioinformatic approach. Overall, the results support the development of novel vaccines that contain OMVs obtained from bacteria grown to simulate the in vivo environment, and possibly biofilm matrix, to prevent diseases due to bacterial pathogens.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Bos Taurus (bovine)

TISSUE(S): Blood Cell, Cell Culture

SUBMITTER: Qin Fu

LAB HEAD: Qin Fu

PROVIDER: PXD061987 | Pride | 2025-05-15

REPOSITORIES: Pride

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			Action	DRS
	YungfuChang10446152_B_1_fourFraction.msf	Msf
	YungfuChang10446152_B_1_fourFractions.mgf	Mgf
	YungfuChang10446152_B_2_fourFractions.mgf	Mgf
	YungfuChang10446152_B_2_fourFractions.msf	Msf
	YungfuChang10446152_B_blue4_1.raw	Raw

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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.

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Protein composition of the biofilm matrix and the outer membrane vesicles (OMVs) during iron-sufficient and iron-restricted growth.

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