Characterization of the <i>Coxiella burnetii suc</i>B Gene Encoding an Immunogenic Dihydrolipoamide Succinyltransferase

Nguyen, Sa Van; To, Ho; Yamaguchi, Tsuyoshi; Fukushi, Hideto; Hirai, Katsuya

doi:10.1111/j.1348-0421.1999.tb02465.x

Cited by 13 publications

(13 citation statements)

References 25 publications

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“…Therefore, establishing serological diagnosis using specific recombinant proteins is desired to solve these problems. In the case of C. burnetii, the antibody responses to SucB protein have been shown to be detected from Q fever patients (16). Furthermore, the SucB proteins of Brucella species, such as B. ovis and B. melitensis have also been found to react with the sera from naturally infected ram and sheep, respectively (24,27).…”

Section: Expression and Antigenicity Of The B Henselae Sucbmentioning

confidence: 93%

Cloning and Expression of Bartonella henselae sucB Gene Encoding an Immunogenic Dihydrolipoamide Succinyltransferase Homologous Protein

Kabeya

Maruyama

Hirano

et al. 2003

Microbiology and Immunology

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Immunoscreening of a ZAP genomic library of Bartonella henselae strain Houston‐1 expressed in Escherichia coli resulted in the isolation of a clone containing 3.5 kb BamHI genomic DNA fragment. This 3.5 kb DNA fragment was found to contain a sequence of a gene encoding a protein with significant homology to the dihydrolipoamide succinyltransferase of Brucella melitensis (sucB). Subsequent cloning and DNA sequence analysis revealed that the deduced amino acid sequence from the cloned gene showed 66.5% identity to SucB protein of B. melitensis, and 43.4 and 47.2% identities to those of Coxiella burnetii and E. coli, respectively. The gene was expressed as a His‐Nus A‐tagged fusion protein. The recombinant SucB protein (rSucB) was shown to be an immunoreactive protein of about 115 kDa by Western blot analysis with sera from B. henselae‐immunized mice. Therefore the rSucB may be a candidate antigen for a specific serological diagnosis of B. henselae infection.

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Section: Expression and Antigenicity Of The B Henselae Sucbmentioning

confidence: 93%

Cloning and Expression of Bartonella henselae sucB Gene Encoding an Immunogenic Dihydrolipoamide Succinyltransferase Homologous Protein

Kabeya

Maruyama

Hirano

et al. 2003

Microbiology and Immunology

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“…(23,33), Brucella spp. (55,62), and Coxiella burnetii (38), and SucC is considered a diagnostic target as well as a potential vaccine candidate in Leptospira spp. (48).…”

Section: Following Recovery From Sublethal Infection Boosting With Hmentioning

confidence: 99%

Francisella tularensisInfection-Derived Monoclonal Antibodies Provide Detection, Protection, and Therapy

Savitt

Mena-Taboada

Monsalve

et al. 2009

Clin Vaccine Immunol

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Francisella tularensis is the causative agent of tularemia and a potential agent of biowarfare. As an easily transmissible infectious agent, rapid detection and treatment are necessary to provide a positive clinical outcome. As an agent of biowarfare, there is an additional need to prevent infection. We made monoclonal antibodies to the F. tularensis subsp. holarctica live vaccine strain (F. tularensis LVS) by infecting mice with a sublethal dose of bacteria and, following recovery, by boosting the mice with sonicated organisms. The response to the initial and primary infection was restricted to immunoglobulin M antibody directed solely against lipopolysaccharide (LPS). After boosting with sonicated organisms, the specificity repertoire broadened against protein antigens, including DnaK, LpnA, FopA, bacterioferritin, the 50S ribosomal protein L7/L12, and metabolic enzymes. These monoclonal antibodies detect F. tularensis LVS by routine immunoassays, including enzyme-linked immunosorbent assay, Western blot analysis, and immunofluorescence. The ability of the antibodies to protect mice from intradermal infection, both prophylactically and therapeutically, was examined. An antibody to LPS which provides complete protection from infection with F. tularensis LVS and partial protection from infection with F. tularensis subsp. tularensis strain SchuS4 was identified. There was no bacteremia and reduced organ burden within the first 24 h when mice were protected from F. tularensis LVS infection with the anti-LPS antibody. No antibody that provided complete protection when administered therapeutically was identified; however, passive transfer of antibodies against LPS, FopA, and LpnA resulted in 40 to 50% survival of mice infected with F. tularensis LVS.

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“…Recently, two-dimensional electrophoresis, immunoblotting, and N-terminal microsequencing have considerably facilitated the identification of immunogenic proteins in ovine brucellosis (15,16). Among the proteins identified by these methods, one with an apparent molecular mass of 45 kDa was recognized by sera from Brucella-infected sheep, and its N-terminal sequence showed homology to a dihydrolipoamide succinyltransferase (SucB) described in many bacteria (2,5,9,13,19). A monoclonal antibody (MAb) was raised against this protein (16) to allow easy screening of genomic libraries to clone the corresponding gene.…”

mentioning

confidence: 99%

Cloning, Nucleotide Sequence, and Expression of the Brucella melitensis sucB Gene Coding for an Immunogenic Dihydrolipoamide Succinyltransferase Homologous Protein

et al. 2001

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The Brucella melitensis sucB gene encoding the dihydrolipoamide succinyltransferase (E2o) enzyme (previously identified as an immunogenic protein in infected sheep) was cloned and sequenced. The amino acid sequence predicted from the cloned gene revealed 88.8 and 51.2% identity to the dihydrolipoamide succinyltransferase SucB protein from Brucella abortus and Escherichia coli, respectively. Sera from naturally infected sheep showed antibody reactivity against the recombinant SucB protein.Brucella spp. are gram-negative, facultative intracellular bacterial pathogens that cause brucellosis, an infectious disease affecting animals and humans. Brucella melitensis is the most important species involved in ovine and caprine brucellosis, which is characterized by abortion, low production, and infertility in infected animals. B. melitensis is also the most pathogenic species for humans.One of the principal aims in brucellosis research is the identification of Brucella antigens eliciting humoral and/or cellmediated responses, which might be of interest for the development of diagnostic tests or subcellular vaccines that avoid the drawbacks of those currently used. B. melitensis Rev 1, a live attenuated vaccine strain that is currently used in sheep and goats, has been successful in disease eradication and control programs in some countries (1). However, there have been significant problems associated with its use. The most important among them are the residual virulence of Rev1 for humans and the development of agglutinating antibodies in animals vaccinated as adults which are indistinguishable from those elicited by natural infection (8). The construction of new brucellosis vaccines and associated diagnostic tests lacking these indesirable properties would be of great interest to veterinary medicine.A number of immunogenic proteins have been previously identified by immunoblotting, such as the BP26 protein, and are currently being considered for the development of new diagnostic tests for ovine brucellosis (3,6,7,10). Recently, two-dimensional electrophoresis, immunoblotting, and N-terminal microsequencing have considerably facilitated the identification of immunogenic proteins in ovine brucellosis (15,16). Among the proteins identified by these methods, one with an apparent molecular mass of 45 kDa was recognized by sera from Brucella-infected sheep, and its N-terminal sequence showed homology to a dihydrolipoamide succinyltransferase (SucB) described in many bacteria (2,5,9,13,19). A monoclonal antibody (MAb) was raised against this protein (16) to allow easy screening of genomic libraries to clone the corresponding gene. The present report describes the cloning and the nucleotide sequence of the gene termed sucB encoding dihydrolipoamide succinyltransferase (E2o), an enzyme of the ␣-ketoglutarate dehydrogenase complex, and its expression in Escherichia coli.Specificity of the anti-SucB MAb. The MAb raised against Brucella SucB did not cross-react with E. coli and other bacteria closely genetically related to Brucella...

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Characterization of the Coxiella burnetii sucB Gene Encoding an Immunogenic Dihydrolipoamide Succinyltransferase

Abstract: Abstract:The

Cited by 13 publications

References 25 publications

Cloning and Expression of Bartonella henselae sucB Gene Encoding an Immunogenic Dihydrolipoamide Succinyltransferase Homologous Protein

Cloning and Expression of Bartonella henselae sucB Gene Encoding an Immunogenic Dihydrolipoamide Succinyltransferase Homologous Protein

Francisella tularensisInfection-Derived Monoclonal Antibodies Provide Detection, Protection, and Therapy

Cloning, Nucleotide Sequence, and Expression of the Brucella melitensis sucB Gene Coding for an Immunogenic Dihydrolipoamide Succinyltransferase Homologous Protein

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