Humoral antibody response and protective immunity in swine following immunization with the 104-kilodalton hemolysin of Actinobacillus pleuropneumoniae

Devenish, John; Rosendal, S; Bossé, Janine T.

doi:10.1128/iai.58.12.3829-3832.1990

Cited by 66 publications

(30 citation statements)

References 11 publications

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“…Haemolysins have often been implicated as virulence factors of several Grampositive and Gram-negative bacteria (DEVENISH et al, 1990;JOHNSON, 1991, HAGUE et a]., 1992.…”

Section: Discussionmentioning

confidence: 99%

Purification and Further Characterization of a Haemolysin of Actinomyces pyogenes

Ding

Lämmler

1996

Journal of Veterinary Medicine, Series B

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Summary A haemolysin produced by Actinomyces pyogenes ATCC 8164 was purified from culture supernatant by ammonium sulphate and polyethylene glycol precipitation, ion‐exchange chromatography on DEAE‐Sephacel, and fast‐protein‐liquid‐chromatography on Superose 12 prep grade. The purified haemolysin, designated as pyolysin, displayed a single band on poly‐acrylamide gel electrophoresis, indicating a molecular weight of 55000. Additionally, using gel filtration, the same molecular weight was estimated. Further studies of the eluate of ion‐exchange chromatography using isoelectric focusing also revealed a single protein band at pH 9.38 with haemolytic activity. A specific antiserum produced against pyolysin inhibited the haemolytic activity. The purity of the isolated protein was also determined by Western Blot analysis with antiserum obtained from a cow inoculated with culture supernatant from A. pyogenes and Peptococcus indolicus. The isolated pyolysin appeared to be heat‐labile and displayed cytotoxic effects on poly‐morphonuclear leucocytes and on pTK2 kidney cells.

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“…Haemolysins have often been implicated as virulence factors of several Grampositive and Gram-negative bacteria (DEVENISH et al, 1990;JOHNSON, 1991, HAGUE et a]., 1992.…”

Section: Discussionmentioning

confidence: 99%

Purification and Further Characterization of a Haemolysin of Actinomyces pyogenes

Ding

Lämmler

1996

Journal of Veterinary Medicine, Series B

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“…In addition, unlike the SD vaccinated pigs which needed in one case two doses to achieve a significantly higher score than the controls (Table 1), the ScientificScientificScientificScientific agreement with the findings of other researchers. 5,26 The immunoblot results also illustrate a possible reason why both the SD and subunit vaccines failed to provide protection against the serovar 15 challenge. Both vaccines failed to elicit, in vaccinated pigs, detectable immunoblot reactions, using the serovar 15 antigen, to ApxIII.…”

Section: Treatmentmentioning

confidence: 99%

An evaluation of the role of antibodies toActinobacillus pleuropneumoniaeserovar 1 and 15 in the protection provided by sub‐unit and live streptomycin‐dependent pleuropneumonia vaccines

Tumamao¹,

Bowles²,

Bosch³

et al. 2004

Aust Veterinary J

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Objective To evaluate the serological response of pigs receiving either the Porcilis APP vaccine or a modified live vaccine based on a streptomycin‐dependent (SD) strain of Actinobacillus pleuropneumoniae, and then challenged with an Australian isolate of A pleuropneumoniae of either serovar 1 or 15 as a means of understanding the protection provided by both vaccines against serovar 1 but not against serovar 15. Design The serological tests evaluated were serovarspecific polysaccharide ELISA tests (for serovar 1 and 15), ELISA tests for antibodies to three A pleuropneumoniae toxins (ApxI, ApxII and ApxIII) as well as to a 42 kDa outer membrane protein (OMP), a haemolysin neutralisation (HN) assay and immunoblotting. The tests were used to detect antibodies in vaccinated pigs that had been shown to be protected against serovar 1 but not serovar 15. Results In the polysaccharide antigen ELISA assays, both vaccines resulted in a significant rise in the titre in the serovar 1 ELISA but not the serovar 15 ELISA. The Porcilis APP vaccinated pigs showed a significant response in the ApxI, ApxIII and 42 kDa OMP ELISA. In the ApxII ELISA, all pigs tested (the Porcilis APP vaccinates and the controls) were positive on entry to the trial. In the HN assay, the Porcilis APP vaccinated pigs showed a significant response after one dose while the SD vaccinated pigs required two doses of vaccine before a marked rise in titre was induced. Immunoblotting revealed that neither vaccine generated antibodies that recognised the ApxIII produced by serovar 15. Conclusions The failure of these vaccines to provide protection against serovar 15 may be due to novel virulence factors possessed by serovar 15, significant differences between the ApxIII toxin of serovar 15 and those present in the Porcilis APP vaccine or failure by both vaccines to induce antibodies to the serovar 15 specific polysaccharide.

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“…To improve the performance of first generation inactivated vaccines, other targets have been studied recently [9,10]. The most promising vaccine candidates are cross protective antigens; typically these are immunogenic markers of pathogens highly conserved across multiple serovars [11].…”

Section: Introductionmentioning

confidence: 99%

Galactose-1-phosphate uridyltransferase (GalT), an in vivo-induced antigen of Actinobacillus pleuropneumoniae serovar 5b strain L20, provided immunoprotection against serovar 1 strain MS71

et al. 2018

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GALT is an important antigen of Actinobacillus pleuropneumoniae (APP), which was shown to provide partial protection against APP infection in a previous study in our lab. The main purpose of the present study is to investigate GALT induced cross-protection between different APP serotypes and elucidate key mechanisms of the immune response to GALT antigenic stimulation. Bioinformatic analysis demonstrated that galT is a highly conserved gene in APP, widely distributed across multiple pathogenic strains. Homologies between any two strains ranges from 78.9% to 100% regarding the galT locus. Indirect enzyme-linked immunosorbent assay (ELISA) confirmed that GALT specific antibodies could not be induced by inactivated APP L20 or MS71 whole cell bacterin preparations. A recombinant fusion GALT protein derived from APP L20, however has proven to be an effective cross-protective antigen against APP sevorar 1 MS71 (50%, 4/8) and APP sevorar 5b L20 (75%, 6/8). Histopathological examinations have confirmed that recombinant GALT vaccinated animals showed less severe pathological signs in lung tissues than negative controls after APP challenge. Immunohistochemical (IHC) analysis indicated that the infiltration of neutrophils in the negative group is significantly increased compared with that in the normal control (P<0.001) and that in surviving animals is decreased compared to the negative group. Anti-GALT antibodies were shown to mediate phagocytosis of neutrophils. After interaction with anti-GALT antibodies, survival rate of APP challenged vaccinated animals was significantly reduced (P<0.001). This study demonstrated that GALT is an effective cross-protective antigen, which could be used as a potential vaccine candidate against multiple APP serotypes.

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Humoral antibody response and protective immunity in swine following immunization with the 104-kilodalton hemolysin of Actinobacillus pleuropneumoniae

Cited by 66 publications

References 11 publications

Purification and Further Characterization of a Haemolysin of Actinomyces pyogenes

Purification and Further Characterization of a Haemolysin of Actinomyces pyogenes

An evaluation of the role of antibodies toActinobacillus pleuropneumoniaeserovar 1 and 15 in the protection provided by sub‐unit and live streptomycin‐dependent pleuropneumonia vaccines

Galactose-1-phosphate uridyltransferase (GalT), an in vivo-induced antigen of Actinobacillus pleuropneumoniae serovar 5b strain L20, provided immunoprotection against serovar 1 strain MS71

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