Genome-Wide Analysis and Characterization of the Riemerella anatipestifer Putative T9SS Secretory Proteins with a Conserved C-Terminal Domain

Chen, Zongchao; Niu, Pei; Ren, Xiaomei; Han, Wenlong; Shen, Ruyu; Zhu, Min; Yu, Yang; Yu, Shuang

doi:10.1128/jb.00073-22

Cited by 4 publications

(1 citation statement)

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“…The type IX secretion system (T9SS) is a complex translocon found in many species of the phylum Bacteroidetes and is associated with bacterial gliding motility, protein secretion, and virulence [ 15 – 18 ]. Bacteria use the T9SS to secrete many cargo proteins, such as SspA, MPPE, and AS87_RS02955, which have been confirmed to be virulence factors [ 19 – 22 ]. SspA was identified as a serine protease with functions in bacterial protease activity and virulence.…”

Section: Introductionmentioning

confidence: 99%

Occludin and collagen IV degradation mediated by the T9SS effector SspA contributes to blood–brain barrier damage in ducks during Riemerella anatipestifer infection

Chen,

Zhu,

Liu

et al. 2024

Vet Res

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Riemerella anatipestifer infection is characterized by meningitis with neurological symptoms in ducklings and has adversely affected the poultry industry. R. anatipestifer strains can invade the duck brain to cause meningitis and neurological symptoms, but the underlying mechanism remains unknown. In this study, we showed that obvious clinical symptoms, an increase in blood‒brain barrier (BBB) permeability, and the accumulation of inflammatory cytokines occurred after intravenous infection with the Yb2 strain but not the mutant strain Yb2ΔsspA, indicating that Yb2 infection can lead to cerebrovascular dysfunction and that the type IX secretion system (T9SS) effector SspA plays a critical role in this pathological process. In addition, we showed that Yb2 infection led to rapid degradation of occludin (a tight junction protein) and collagen IV (a basement membrane protein), which contributed to endothelial barrier disruption. The interaction between SspA and occludin was confirmed by coimmunoprecipitation. Furthermore, we found that SspA was the main enzyme mediating occludin and collagen IV degradation. These data indicate that R. anatipestifer SspA mediates occludin and collagen IV degradation, which functions in BBB disruption in R. anatipestifer-infected ducks. These findings establish the molecular mechanisms by which R. anatipestifer targets duckling endothelial cell junctions and provide new perspectives for the treatment and prevention of R. anatipestifer infection.

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Section: Introductionmentioning

confidence: 99%

Occludin and collagen IV degradation mediated by the T9SS effector SspA contributes to blood–brain barrier damage in ducks during Riemerella anatipestifer infection

Chen,

Zhu,

Liu

et al. 2024

Vet Res

Self Cite

View full text Add to dashboard Cite

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Riemerella anatipestifer GldG is necessary for secretion of effectors by type IX secretion system

Chen

Han

Zhu

et al. 2023

Veterinary Microbiology

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Riemerella anatipestifer Endonuclease I displays enzymatic activity and is associated with bacterial virulence

Shen

Chen

et al. 2023

Veterinary Microbiology

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Genome-Wide Analysis and Characterization of the Riemerella anatipestifer Putative T9SS Secretory Proteins with a Conserved C-Terminal Domain

Abstract: Riemerella anatipestifer T9SS plays an important role in bacterial virulence. We have previously reported nine R. anatipestifer T9SS-secreted proteins and clarified the function of the metallophosphoesterase.

Cited by 4 publications

References 50 publications

Occludin and collagen IV degradation mediated by the T9SS effector SspA contributes to blood–brain barrier damage in ducks during Riemerella anatipestifer infection

Occludin and collagen IV degradation mediated by the T9SS effector SspA contributes to blood–brain barrier damage in ducks during Riemerella anatipestifer infection

Riemerella anatipestifer GldG is necessary for secretion of effectors by type IX secretion system

Riemerella anatipestifer Endonuclease I displays enzymatic activity and is associated with bacterial virulence

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