A 39kDa protein mediates adhesion of avian Pasteurella multocida to chicken embryo fibroblast cells

Borrathybay, Entomack; Sawada, Takuo; Kataoka, Yuki; Ohtsu, Naoko; Takagi, Masami; Nakamura, Shigeyuki; Kawamoto, Eiichi

doi:10.1016/j.vetmic.2003.09.010

Cited by 22 publications

(24 citation statements)

References 15 publications

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“…A protein of similar molecular mass (39 kDa) was identified in the P. multocida A:3 strain P1059; its expression was shown to correlate with the presence and amount of capsule present on the cell (Borrathybay et al , 2003b; Ali et al , 2004a). Pasteurella multocida can adhere to, and invade, chicken embryo fibroblasts, and this adherence was inhibited by both monoclonal and polyclonal antibodies raised against the 39 kDa protein (Borrathybay et al , 2003a; Al‐haj Ali et al , 2004; Ali et al , 2004a, b). Passive immunization of mice with a monoclonal antibody against the 39 kDa protein or active immunization with affinity purified 39 kDa protein, demonstrated that antibodies raised against this protein were cross‐protective against serovars A:1 and A:3 (Ali et al , 2004a, b).…”

Section: Virulence Factorsmentioning

confidence: 99%

Pasteurella multocida pathogenesis: 125 years after Pasteur

Harper

Boyce

Adler

2006

FEMS Microbiology Letters

362

300

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Pasteurella multocida was first shown to be the causative agent of fowl cholera by Louis Pasteur in 1881. Since then, this Gram-negative bacterium has been identified as the causative agent of many other economically important diseases in a wide range of hosts. The mechanisms by which these bacteria can invade the mucosa, evade innate immunity and cause systemic disease are slowly being elucidated. Key virulence factors identified to date include capsule and lipopolysaccharide. The capsule is clearly involved in bacterial avoidance of phagocytosis and resistance to complement, while complete lipopolysaccharide is critical for bacterial survival in the host. A number of other virulence factors have been identified by both directed and random mutagenesis, including Pasteurella multocida toxin (PMT), putative surface adhesins and iron acquisition proteins. However, it is likely that many key virulence factors are yet to be identified, including those required for initial attachment and invasion of host cells and for persistence in a relatively nutrient poor and hostile environment.

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Section: Virulence Factorsmentioning

confidence: 99%

Pasteurella multocida pathogenesis: 125 years after Pasteur

Harper

Boyce

Adler

2006

FEMS Microbiology Letters

362

300

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“…In addition, the secretory IgA was determined by an IgA Chicken ELISA test kit (ab157619, Abcam ® , Cambridge, UK). Chicken sera or tracheal lavage suspensions against rOmpH from the previous study (Borrathybay et al, 2003) were used as positive controls. Absorbance values were recorded at a wavelength of 450 nm using an ELISA reader (Immuno Mini NJ 2300, Intermed, Osaka, Japan).…”

Section: Enzyme-linked Immunosorbent Assaymentioning

confidence: 99%

“…The OmpH of P. multocida strain X-73 plays an important role as a vaccine candidate for pasteurellosis (Luo et al, 1997;Sthitmatee et al, 2008;Thanasarasakulpong et al, 2015). Our previous studies demonstrated that the outer membrane protein H of P. multocida strain X-73 (serovar A:1) is a capsule-associated antigen and a cross-protective antigen among P. multocida capsular serogroup A strains (Ali et al, 2004a(Ali et al, , 2004bBorrathybay et al, 2003). The recombinant outer membrane protein (rOmpH) of strain X-73 was prepared in Escherichia coli and purified by electroelution (Thanasarasakulpong et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Cross-protection conferred by immunization with an rOmpH-based intranasal fowl cholera vaccine

et al. 2017

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A previous study demonstrated that a recombinant outer membrane protein H (rOmpH)-based intranasal fowl cholera vaccine elicited efficient homologous protection against the Pasteurella multocida strain X-73 (A:1) in chickens. The present study aimed to determine the cross-protectivity against heterologous P. multocida strains. The rOmpH was purified via electroelution and formulated with two kinds of adjuvants. The vaccine formulations in a total volume of 100 µl were 100 µg rOmpH with 3 µg of Escherichia coli enterotoxin B or 10 µg of CpG ODN2007. Chickens were assigned to three experimental groups depending on bacterial strain challenge exposure as well as three control groups. The chickens were immunized intranasally three times at three-week intervals. Challenge exposures were conducted by inoculation with homologous strain X-73 or heterologous strains P-1059 (A:3) or P-1662 (A:4) at four weeks after the final immunization. The specific antibody against rOmpH was produced in vaccinated birds. Sera IgY and secretory IgA antibody titres were significantly increased (P < 0.05) post-immunization. The stimulation index values of the vaccinated groups were significantly different from stimulation index values of the non-vaccinated groups (P < 0.05). Chicken survival rates after exposure to avian P. multocida strains ranged from 70% to 100%. There was no significant difference in protection between two kinds of adjuvants in vaccine formulations. Statistical analysis indicated no significant differences in protection among avian P. multocida strains challenge exposure. We conclude that an in-house rOmpH-based intranasal fowl cholera vaccine produced efficient cross-protectivity against heterologous strains of P. multocida.

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“…Adherence factors such as pili play a role in adherence to cell surfaces . OMPs also participate in invasion and intracellular survival to evade of host defense . Even though these virulence factors are known, it is still unclear how P. multocida exacerbates pneumonia and whether it helps to create multiple infections.…”

Section: Introductionmentioning

confidence: 99%

Identification of an antilymphocyte transformation substance from Pasteurella multocida

Tanabe

Fukuzawa

Amatatsu

et al. 2019

Microbiology and Immunology

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Pasteurella multocida is one of the most important bacteria responsible for diseases of animals. Crude extracts from sonicated P. multocida strain Dainai‐1, which is serotype A isolated from bovine pneumonia, were found to inhibit proliferation of mouse spleen cells stimulated with Con A. The crude extract was purified by cation and anion exchange chromatography and hydroxyapatite chromatography. Its molecular weight was 27 kDa by SDS‐PAGE and it was named PM27. PM27 was found to inhibit proliferation of mouse spleen cells stimulated with Con A as effectively as did the crude extract; however, its activity was lost after heating to 100°C for 20 min. PM27 did not directly inhibit proliferation of HT‐2 cells, which are an IL‐2‐dependent T cell line, nor did it modify IL‐2 production by Con A‐stimulated mouse spleen cells. The N‐terminal amino acid sequence of PM27 was determined and BLAST analysis revealed its identity to uridine phosphorylase (UPase) from P. multocida. UPase gene from P. multocida Dainai‐1 was cloned into expression vector pQE‐60 in Escherichia coli XL‐1 Blue. Recombinant UPase (rUPase) tagged with His at the C‐terminal amino acid was purified with Ni affinity chromatography. rUPase was found to inhibit proliferation of mouse spleen cells stimulated with Con A; however, as was true for PM27, its activity was lost after heating to 100°C for 20 min. Thus, PM27/UPase purified from P. multocida has significant antiproliferative activity against Con A‐stimulated mouse spleen cells and may be a virulence factor.

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A 39kDa protein mediates adhesion of avian Pasteurella multocida to chicken embryo fibroblast cells

Cited by 22 publications

References 15 publications

Pasteurella multocida pathogenesis: 125 years after Pasteur

Pasteurella multocida pathogenesis: 125 years after Pasteur

Cross-protection conferred by immunization with an rOmpH-based intranasal fowl cholera vaccine

Identification of an antilymphocyte transformation substance from Pasteurella multocida

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