Riemerella anatipestifer AS87_RS02955 Acts as a Virulence Factor and Displays Endonuclease Activity

Zhu, Min; Chen, Zongchao; Shen, Ruyu; Niu, Pei; Feng, Yating; Liú, Dan; Yu, Shuang

doi:10.1128/aem.01276-22

Cited by 5 publications

(1 citation statement)

References 62 publications

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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

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A novel bivalent inactivated vaccine for ducks against Riemerella anatipestifer based on serotype distribution in southern China

Liang,

Li,

Yang

et al. 2024

Poultry Science

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A journey with type IX secretion system effectors: selection, transport, processing and activities

et al. 2023

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The type IX secretion system (T9SS) is a multiprotein machine distributed in Bacteroidota and responsible for the secretion of various proteins across the outer membrane. Secreted effectors can be either delivered into the medium or anchored to the cell surface. The T9SS is composed of a transenvelope complex consisting of proton-motive force-dependent motors connected to a membrane-associated ring and outer membrane translocons, and a cell-surface anchoring complex that processes effectors once translocated. The T9SS is involved in pathogenesis, metal acquisition, carbohydrate degradation, S-layer biogenesis and gliding motility. The broad spectrum of functions is linked to a highly versatile repertoire of effectors including metallophores, enzymes, toxins and adhesins, that all possess specific signatures to be recruited and transported by the apparatus. This review summarizes the current knowledge on T9SS substrate secretion signals, transport, processing and activities.

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Riemerella anatipestifer AS87_RS02955 Acts as a Virulence Factor and Displays Endonuclease Activity

Abstract: R. anatipestifer AS87_RS02955 was identified as a novel T9SS effector and displayed a nonspecific endonuclease activity in this study. The protein did not contain a conserved His-Asn-His motif structure, which is similar to the endonuclease from Prevotella sp.

Cited by 5 publications

References 62 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

A novel bivalent inactivated vaccine for ducks against Riemerella anatipestifer based on serotype distribution in southern China

A journey with type IX secretion system effectors: selection, transport, processing and activities

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