Nasal immunization with major epitope-containing ApxIIA toxin fragment induces protective immunity against challenge infection with Actinobacillus pleuropneumoniae in a murine model

Seo, Ki-Weon; Kim, Sae-Hae; Park, Jisang; Son, Young‐Ok; Yoo, Han Sang; Lee, Kyung-Yeol; Jang, Yong-Suk

doi:10.1016/j.vetimm.2012.10.011

Cited by 18 publications

(19 citation statements)

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“…pleuropneumoniae infection [24, 25]. Specific-pathogen-free, six-week-old female BALB/c mice (Beijing Vital River Laboratory Animal Co., Ltd.) were used for virulence evaluation of A .…”

Section: Methodsmentioning

confidence: 99%

Pyridoxal phosphate synthases PdxS/PdxT are required for Actinobacillus pleuropneumoniae viability, stress tolerance and virulence

Xie

Wang

et al. 2017

PLoS ONE

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Pyridoxal 5’-phosphate (PLP) is an essential cofactor for numerous enzymes involved in a diversity of cellular processes in living organisms. Previous analysis of the Actinobacillus pleuropneumoniae S-8 genome sequence revealed the presence of pdxS and pdxT genes, which are implicated in deoxyxylulose 5-phosphate (DXP)-independent pathway of PLP biosynthesis; however, little is known about their roles in A. pleuropneumoniae pathogenicity. Our data demonstrated that A. pleuropneumoniae could synthesize PLP by PdxS and PdxT enzymes. Disruption of the pdxS and pdxT genes rendered the pathogen auxotrophic for PLP, and the defective growth as a result of these mutants was chemically compensated by the addition of PLP, suggesting the importance of PLP production for A. pleuropneumoniae growth and viability. Additionally, the pdxS and pdxT deletion mutants displayed morphological defects as indicated by irregular and aberrant shapes in the absence of PLP. The reduced growth of the pdxS and pdxT deletion mutants under osmotic and oxidative stress conditions suggests that the PLP synthases PdxS/PdxT are associated with the stress tolerance of A. pleuropneumoniae. Furthermore, disruption of the PLP biosynthesis pathway led to reduced colonization and attenuated virulence of A. pleuropneumoniae in the BALB/c mouse model. The data presented in this study reveal the critical role of PLP synthases PdxS/PdxT in viability, stress tolerance, and virulence of A. pleuropneumoniae.

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“…pleuropneumoniae infection [24, 25]. Specific-pathogen-free, six-week-old female BALB/c mice (Beijing Vital River Laboratory Animal Co., Ltd.) were used for virulence evaluation of A .…”

Section: Methodsmentioning

confidence: 99%

Pyridoxal phosphate synthases PdxS/PdxT are required for Actinobacillus pleuropneumoniae viability, stress tolerance and virulence

Xie

Wang

et al. 2017

PLoS ONE

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“…En el presente estudio, la leucotoxina A demostró ser homóloga con la proteína ApxIIA de Actinobacillus pleuropneumoniae (e-value = 0; 65% identidad y 80% de similitud), un patógeno de la familia Pasteurellaceae causante de la pleuroneumonía porcina. ApxIIA, al igual que la leucotoxina A, es una exotoxina de la familia RTX, y su importancia como candidato vacunal ha sido demostrado en recientes estudios (Seo et al, 2013).…”

Section: Discussionunclassified

Análisis Genómico de Mannheimia haemolytica Serotipo A2 para la Identificación de Potenciales Candidatos Vacunales contra la Neumonía en Alpacas

L¹,

Maturrano

A³

2017

Rev. investig. vet. Perú

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RESUMENEl objetivo del presente trabajo fue identificar antígenos inmunoprotectivos en la secuencia genómica de Mannheimia haemolytica serotipo A2 Ovino, aislado de ovino y disponible en las bases de datos, que puedan ser utilizados como potenciales candidatos vacunales contra la neumonía en alpacas. Para ello, se empleó la secuencia completa del genoma de este microorganismo disponible en las bases de datos y mediante el uso de herramientas bioinformáticas se procedió a la búsqueda e identificación de genes candidatos, la anotación funcional, la predicción de la localización subcelular y la identificación de motivos de secuencias, incluyendo dominios transmembrana, peptidos señal de secreción y lipoproteínas. Los factores de virulencia fueron identificados en la base de datos de factores de virulencia (VFDB) y en la base de datos microbiana de virulencia (MvirDB). Los criterios de selección incluyeron proteínas conservadas, secretadas y asociadas a superficie con hélices transmembrana <1. Se realizó la búsqueda de homología de genes con la base de datos de antígenos protectivos (Protegen), permitiendo la identificación de 23 antígenos potencialmente inmunoprotectivos, conservados entre los serotipos virulentos de M. haemolytica y otros patógenos de la familia Pasteurellaceae. Los genes identificados están relacionados con la patogénesis, virulencia y evasión del sistema immune del hospedero y podrían ser grandes candidatos a ser evaluados como potenciales vacunas contra la pasteurelosis neumónica.Palabras clave: Mannheimia haemolytica, pasteurelosis neumónica, vacunología reversa, factores de virulencia, candidatos vacunales inmunoprotectivos

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“…The BALB/c mouse model has been acknowledged as an appropriate one to assess A. pleuropneumoniae infection (Chiang et al, 2009; Seo et al, 2013). Specific-pathogen-free, 6-week-old female BALB/c mice (Beijing Vital River Laboratory Animal Co., Ltd.) were purchased from the VitalRiver Laboratories (VRL, Beijing, China).…”

Section: Methodsmentioning

confidence: 99%

The SapA Protein Is Involved in Resistance to Antimicrobial Peptide PR-39 and Virulence of Actinobacillus pleuropneumoniae

Xie

Wang

et al. 2017

Front. Microbiol.

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Antimicrobial peptides are essential to the innate immune defense of the mammal against bacterial infection. However, pathogenic bacteria have evolved multiple strategies to resist and evade antimicrobial peptides, which is vital to bacterial survival and colonization in hosts. PR-39 is a linear porcine antimicrobial peptide containing 39 amino acid residues with a high proline content. Resistance to antimicrobial peptide PR-39 has been observed in Actinobacillus pleuropneumoniae. However, little is known about the factors required for this resistance. In the present study, PR-39 exposure increased the expression of the sapA gene in A. pleuropneumoniae. The sapA gene, which encodes a putative peptide transport periplasmic protein, was deleted from this bacterium. The ΔsapA mutant showed increased sensitivity to PR-39 compared to the wild-type MD12 and complemented PΔsapA strains. However, the ΔsapA mutant did not exhibit any alterations in outer membrane integrity. Scanning electron microscopy showed that the ΔsapA mutant displayed morphological defects, as indicated by a deformed and sunken shape after PR-39 treatment. In addition, disruption of the SapA protein led to reduced colonization and attenuated virulence of A. pleuropneumoniae in the BALB/c mouse model. Collectively, these data suggest that SapA acts as one mechanism for A. pleuropneumoniae to counteract PR-39-mediated killing. To the best of our knowledge, this is the first study to show a mechanism underlying antimicrobial peptide resistance in A. pleuropneumoniae.

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Nasal immunization with major epitope-containing ApxIIA toxin fragment induces protective immunity against challenge infection with Actinobacillus pleuropneumoniae in a murine model

Cited by 18 publications

References 46 publications

Pyridoxal phosphate synthases PdxS/PdxT are required for Actinobacillus pleuropneumoniae viability, stress tolerance and virulence

Pyridoxal phosphate synthases PdxS/PdxT are required for Actinobacillus pleuropneumoniae viability, stress tolerance and virulence

Análisis Genómico de Mannheimia haemolytica Serotipo A2 para la Identificación de Potenciales Candidatos Vacunales contra la Neumonía en Alpacas

The SapA Protein Is Involved in Resistance to Antimicrobial Peptide PR-39 and Virulence of Actinobacillus pleuropneumoniae

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