Nucleotide sequence of htpB, the Legionella pneumophila gene encoding the 58-kilodalton (kDa) common antigen, formerly designated the 60-kDa common antigen

Sampson, J S; O'Connor, S P; Holloway, Brian P.; Plikaytis, Bonnie B.; Carlone, George M.; Mayer, Leonard W.

doi:10.1128/iai.58.9.3154-3157.1990

Cited by 33 publications

(15 citation statements)

References 24 publications

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“…This family of proteins is immunodominant in infections due to Mycobacteria (Thole and Van der Zee, 1990) and Legionella (Sampson et al, 1986;Plikaytis et al, 1987) and the results reported here confirm its immunodominance in porcine brucellosis. In addition, this group of proteins is known to be cross-reactive, demonstrating sequence homology and serological cross-reactions with a wide range of prokaryotic and eukaryotic organisms (Hoiby, 1975;Shinnick et al, 1988;Thole et al, 1988;Waldinger et al, 1988;Sampson et al, 1990). It is therefore not surprising that the immunodominant 62 kDa protein was also recognized by some sera from pigs infected with Y. enterocolitica 0:9, CFT reactor and CFT negative groups of pigs.…”

Section: Discussionmentioning

confidence: 99%

Immunoblot studies in the differential diagnosis of porcine brucellosis: an immunodominant 62 kDa protein is related to the mycobacterial 65 kDa heat shock protein (HSP-65)

Spencer

Broughton

Hamid

et al. 1994

Veterinary Microbiology

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Smooth Brucella spp. share certain lipopolysaccharide antigens with other bacteria, resulting in serological cross-reactions which can prevent the definitive diagnosis of brucellosis. To identify other antigens with serodiagnostic potential, immunoblot studies following sodium dodecyl sulphate-polyacrylamide gel electrophoresis were carried out. Sera from pigs experimentally infected with Brucella suis and naturally infected feral pigs, sera from pigs from a farm with a known history of Yersinia enterocolitica 0:9 infection, Brucella Complement Fixation Test (CFT) reactor pigs (aetiology unknown) and pigs from consistently Brucella CFT negative farms were examined. Although B. suis infected pigs recognized a total of nine B. melitensis antigens, individual pigs rarely recognized more than three antigens in the range. A 62 kDa antigen was recognized by the majority (73%) of the Brucella infected pigs, but only by 10 to 23% of pigs from the other groups. This antigen was shown to be the Brucella homologue of the ubiquitous 65 kDa heat shock protein (HSP-65) family by immunoblot studies with 14 monoclonal antibodies to the Mycobacterium leprae HSP-65. Only four of these monoclones (Y1.2, ML-30, D7C and IIIC8) identified the B. melitensis 62 kDa protein suggesting that unshared, potentially Brucella specific, regions exist. Sera from Y. enterocolitica 0:9 infected pigs, CFT reactor pigs (aetiology unknown), CFT negative pigs and hyperimmune pig serum raised to Y. enterocolitica 0:9 also recognized B. melitensis antigens, most notably a 17 kDa protein. This antigen appears to be a common cross-reactive protein.

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Section: Discussionmentioning

confidence: 99%

Immunoblot studies in the differential diagnosis of porcine brucellosis: an immunodominant 62 kDa protein is related to the mycobacterial 65 kDa heat shock protein (HSP-65)

Spencer

Broughton

Hamid

et al. 1994

Veterinary Microbiology

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“…The transformants were grown on supplemented Luria-Bertani agar containing 200 jig of cabenicillin per ml, 0.4 mM isopropyl-3-D-thiogalactopyranoside (IPTG), and 0.4 ,ug of 5-bromo-4-chloro-3-indolyl-13-D-galactopyranoside (X-Gal) (Sigma Chemical Co., St. Louis, Mo.). Colonies were screened with a MAb to the 37-kDa protein (41) at a 1/1,000 dilution by colony immunoblot (42). Of the approximately 2,000 colonies screened, 2 immunoreactive clones were found.…”

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Cloning and nucleotide sequence analysis of psaA, the Streptococcus pneumoniae gene encoding a 37-kilodalton protein homologous to previously reported Streptococcus sp. adhesins

et al. 1994

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GenepsaA, which encodes the Streptococcus pneumoniae 37-kDa protein, was cloned in Escherichia coli, and its complete nucleotide sequence was determined. Analysis of the sequence of the 2.4-kb cloned fragment revealed three open reading frames (ORFs). ORF2, which is 933 bp long, was identified as psaA. The two other ORFs identified flankpsaA. ORF1, located upstream ofpsaA, is 836 nucleotides long and encodes a protein with a calculated molecular mass of 29,843 Da. The sequence for ORF3, located downstream of psaA, was only partially determined. Northern (RNA) blot analysis of pneumococcal RNA suggests that psaA4 is transcribed as part of a polycistronic message. Analysis of the primary structure of the protein encoded by this gene indicated significant similarity to two previously reported streptococcal proteins, SsaB (80%o similarity) and FimA (92.3% similarity), from S. sanguis and S. parasanguis, respectively. These two homologous proteins have been shown to be associated with bacterial adhesion, and the possibility of a similar role for PsaA is hypothesized.

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“…The diagnostic value of this antigen, even after defining and isolating Legionella-specific regions of the protein, still remains to be proven. Two Le-gionella CAs, the L. pneumophila CA and the L. micdadai CA, have been cloned and expressed in E. coli, and the respective DNA sequences recently reported (Sampson et al 1990, Hogman et al 1990, Hindersson et al 1990). As a reflection of the extensive cross-reactivity between L. pneumophila serogroups 1 and 6, the reactivities of patients' sera with the two antigen preparations were very similar.…”

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Cross‐reactive Legionella antigens and the antibody response during infection

Bangsborg

Shand²,

Pearlman

et al. 1991

APMIS

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Haiby, N. Cross-reactive Legionella antigens and the antibody response during infection. APMIS 99: 854-865, 1991. In order to define cross-reactive Legionella antigens suitable for diagnostic purposes, we investigated sonicate antigens from two Legionella species, including two serogroups of L. pneumophila. The antigens were reacted with heterologous and homologous rabbit antisera in Western blot. Sera from seven patients with culture-verified L . pneurnophila infection and nine patients with serologically confirmed L . micdudei infection were also investigated for reactivity with the corresponding antigens. Among the cross-reactive Legionella antigens defined, non-specific reactivity in patients' sera with the 58-kDa common antigen (CA) was noted. Specific reactions were observed with the Legionella flagellum antigen and with the macrophage infectivity potentiator (Mip) protein; with both antigens, however, the reactive sera were too few to suggest the use of a single antigen in a diagnostic test.

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Nucleotide sequence of htpB, the Legionella pneumophila gene encoding the 58-kilodalton (kDa) common antigen, formerly designated the 60-kDa common antigen

Cited by 33 publications

References 24 publications

Immunoblot studies in the differential diagnosis of porcine brucellosis: an immunodominant 62 kDa protein is related to the mycobacterial 65 kDa heat shock protein (HSP-65)

Immunoblot studies in the differential diagnosis of porcine brucellosis: an immunodominant 62 kDa protein is related to the mycobacterial 65 kDa heat shock protein (HSP-65)

Cloning and nucleotide sequence analysis of psaA, the Streptococcus pneumoniae gene encoding a 37-kilodalton protein homologous to previously reported Streptococcus sp. adhesins

Cross‐reactive Legionella antigens and the antibody response during infection

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