Evaluation of the protective immunity of Riemerella anatipestifer OmpA

Xu, Xinxin; Xu, Yaohui; Miao, Shuang; Jiang, Pan; Cui, Junsheng; Gong, Yanshan; Tan, P. L.; Du, Xiongming; Islam, Nazrul; Hu, Qinghai

doi:10.1007/s00253-019-10294-3

Cited by 10 publications

(10 citation statements)

References 18 publications

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“…The production process for inactivated vaccines utilizes inactivated bacteria, resulting in suitable safety profiles. Xu et al (2020) reported that prokaryotic ompA protein, as a predominant immunogenic protein of R. anatipestifer , was an immunizing antigen but only provided partial protection against challenge with R. anatipestifer . Studies with deletion strains of R. anatipestifer have shown that the main biochemical characteristics of the ∆ phoP / phoR double gene deletion strain are similar to those of the wild-type R. anatipestifer YM strain, albeit with significantly reduced virulence and host tissue invasion capacity.…”

Section: Discussionmentioning

confidence: 99%

Immunogenicity of live phoP gene deletion strain of Riemerella anatipestifer serotype 1

Li¹,

Zhang²,

Wang³

et al. 2023

Poultry Science

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Section: Discussionmentioning

confidence: 99%

Immunogenicity of live phoP gene deletion strain of Riemerella anatipestifer serotype 1

Li¹,

Zhang²,

Wang³

et al. 2023

Poultry Science

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“…His-tagged B739_0832 protein was purified and used to generate rabbit polyclonal antibody, as described before ( Zhang et al, 2017 ). Whole cell, total membrane, inner membrane, and outer membrane of R. anatipestifer samples were analyzed using Western blot assay; OmpA was used as an outer membrane protein reference, TonB was used as an inner membrane protein reference, and RecA was used as a cytoplasmic protein reference ( Thein et al, 2010 ; Liao et al, 2015 ; Xu et al, 2020 ).…”

Section: Methodsmentioning

confidence: 99%

“…Outer membrane proteins of pathogenic bacteria are generally immunogenic and play important roles in virulence and immunity to bacterial diseases ( Weiser and Gotschlich, 1991 ; Hatfaludi et al, 2010 ). To date, few virulence-associated proteins have been reported in R. anatipestifer , such as outer membrane protein A (OmpA), CAMP cohemolysin, Cas9, and TonB-dependent receptor ( Crasta et al, 2002 ; Hu et al, 2011 ; Liao et al, 2015 ; Wang et al, 2019 ; Xu et al, 2020 ). Outer membrane protein H (OmpH) is a major outer membrane protein, conserved in Gram-negative bacteria ( Hatfaludi et al, 2010 ).…”

Section: Introductionmentioning

confidence: 99%

Putative Riemerella anatipestifer Outer Membrane Protein H Affects Virulence

Gao

Wang

et al. 2021

Front. Microbiol.

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Riemerella anatipestifer causes serious contagious disease in ducks, geese, and other fowl. However, as a harmful pathogen causing significant economic losses in the poultry industry, R. anatipestifer is still poorly understood for its pathogenesis mechanisms. In a previous study, we developed an indirect ELISA method for detecting R. anatipestifer infection using B739_0832 protein, a putative outer membrane protein H (OmpH) that is conserved among different serotypes of R. anatipestifer. Although OmpH in some pathogenic bacteria, such as Pasteurella, has been reported as a virulence factor, it is still not clear whether B739_0832 protein contributes to the virulence of R. anatipestifer. In this study, we confirmed that B739_0832 protein in R. anatipestifer localizes to the outer membrane. We constructed a B739_0832 deletion mutant strain (ΔB739_0832) and assayed various effects from the deletion of B739_0832. ΔB739_0832 strain had a similar growth rate to wild-type R. anatipestifer CH-1. However, the survival rate of ducklings in 10 days after infection from ΔB739_0832 strain was 50%, whereas no ducklings survived from wild-type R. anatipestifer infection. Furthermore, the median lethal dose (LD50) of the ΔB739_0832 strain was approximately 150 times higher than that of the wild-type strain. Pathology examinations on infected ducklings found that, at 36 h after infection, bacterial loads in blood, liver, and brain tissues from ΔB739_0832-infected ducklings were considerably lower than those from wild-type infected ducklings. These results demonstrate that the B739_0832 protein contributes to the virulence of R. anatipestifer CH-1.

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“…The recombinant proteins rRiean_0317, rRiean_0653, and rRiean_1143 were expressed in E. coli cells mainly in the soluble form, while rRiean_1561 and rRiean_0790 were expressed mainly in inclusion bodies. The soluble recombinant proteins rRiean_0317, rRiean_0653, and rRiean_1143 were purified by Ni-iminodiacetic acid affinity chromatography (Detai Bio-Tech (Nanjing) Co., Ltd., Nanjing, China), and the recombinant fusion proteins rRiean_1561 and rRiean_0790 were obtained after washing and dissolution of the inclusion bodies, purification by affinity chromatography, and refolding as previously described [19]. All purified recombinant proteins were soluble in solution buffer (50 mM Tris [pH 8.0] and 150 mM NaCl) and the concentration of each recombinant protein solution was measured using the BCA Protein Assay kit (Pierce Biotechnology, Waltham, MA, USA).…”

Section: Expression Of Rriean_1561 Rriean_1143 Rriean_0790 Rriean_mentioning

confidence: 99%

“…The hemolytic activities of the WT SX strain, mutant strains M2 and M18, and complemented strains were measured on duck blood agar as described previously [4], and the hemolytic zones generated by these strains were observed. The hemolytic activities of the recombinant proteins rRiean_0317, rRiean_0790, rRiean_1027 (rOmpA1467) [19], rRiean_0653, rRiean_1143, and rRiean_1561 were also monitored on duck blood agar as described previously [4]. The solution buffer was used as a negative control.…”

Section: Hemolytic Activities Of the Complemented Strains And Recombimentioning

confidence: 99%

Identification of genetic determinants of hemolytic activity of Riemerella anatipestifer using random transposon mutagenesis

Sun

Xue

et al. 2021

Vet Res

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Riemerella anatipestifer causes epizootic infectious disease in poultry resulting in serious economic losses especially to the duck industry. In our previous study, R. anatipestifer was found to lyse duck erythrocytes in vitro. In the present study, a random Tn4351 mutagenesis library of hemolytic R. anatipestifer strain SX containing 4000 mutants was constructed to investigate the genetic basis of hemolytic activity. Thirty mutants with reduced hemolytic activity and one with increased hemolytic activity were screened and insertions in 24 genes were identified. Of these genes, four were predicted to encode outer membrane proteins, one encoded a cytoplasmic membrane protein, 11 encoded cytoplasmic proteins, and eight encoded proteins with unknown locations. Based on current annotations of the R. anatipestifer genomes, of the 24 genes, 7 (29.17%) were involved in iron utilization. The hemolytic activities of the complemented strains M2 (pRES-Riean_0790) and M18 (pRES-Riean_0653) were restored, indicating that both Riean_0653 and Riean_0790 are involved in the hemolytic activity of strain SX. However, the recombinant proteins rRiean_0317, rRiean_0790, rRiean_0653, rRiean_1027, rRiean_1143, and rRiean_1561 had no hemolytic activity, suggesting that none were hemolysins.

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Evaluation of the protective immunity of Riemerella anatipestifer OmpA

Cited by 10 publications

References 18 publications

Immunogenicity of live phoP gene deletion strain of Riemerella anatipestifer serotype 1

Immunogenicity of live phoP gene deletion strain of Riemerella anatipestifer serotype 1

Putative Riemerella anatipestifer Outer Membrane Protein H Affects Virulence

Identification of genetic determinants of hemolytic activity of Riemerella anatipestifer using random transposon mutagenesis

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