Hemin-Binding Surface Protein from
            <i>Bartonella quintana</i>

Carroll, James A.; Coleman, Sherry A.; Smitherman, Laura S.; Minnick, Michael F.

doi:10.1128/iai.68.12.6750-6757.2000

Cited by 57 publications

(92 citation statements)

References 63 publications

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“…These steps decreased the formation of membrane hybrids and increased the yield of purified OM and IM. Centrifugation of the sucrose gradient yielded three membrane bands with densities of 1.20, 1.15, and 1.13 g/cm 3 . Initially, the isolated membrane fractions were analyzed by SDS-PAGE, and the high-and low-density fractions had distinct protein profiles ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…To localize these antigens, purified OM with little contamination from other subcellular components was required. Initially, subcellular fractions were isolated by isopycnic centrifugation using a technique developed for blood agar-grown B. quintana (3). However, the densities of the B. henselae membrane fractions differed from those of B. quintana.…”

Section: Resultsmentioning

confidence: 99%

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Predominant Outer Membrane Antigens of Bartonella henselae

Chenoweth

Greene

Krause³

et al. 2004

Infect Immun

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A hallmark of Bartonella henselae is persistent bacteremia in cats despite the presence of a vigorous host immune response. To understand better the long-term survival of B. henselae in cats, we examined the feline humoral immune response to B. henselae outer membrane (OM) proteins in naturally and experimentally infected cats. Initially, a panel of sera (n ‫؍‬ 42) collected throughout North America from naturally infected cats was used to probe B. henselae total membranes to detect commonly recognized antigens. Twelve antigens reacted with sera from at least 85% of cats, and five were recognized by sera from all cats. To localize these antigens further, OMs were purified on discontinuous sucrose density step gradients. Each membrane fraction (OM, hybrid or inner membrane [IM]) contained less than 1% of the total malate dehydrogenase activity (soluble marker), indicating very little contamination by cytoplasmic proteins. FtsI, an integral IM cell division protein, was used to identify the low-density fraction ( ‫؍‬ 1.13 g/cm 3 ) as putative IM (<5% of the total FtsI localized to the high-density fraction) while lipopolysaccharide (LPS) and Pap31, a homolog of the Bartonella quintana heme-binding protein A (HbpA), defined the high-density fraction ( ‫؍‬ 1.20 g/cm 3 ) as putative OM. Additionally, little evidence of cross-contamination between the IM and OM was evident by two-dimensional gel electrophoresis. When purified OMs were probed with feline sera, antigenic proteins profiles were very similar to those observed with total membranes, indicating that many, but not all, of the immunoreactive proteins detected in the initial immunoblots were OM components. Interestingly, two-dimensional immunoblots indicated that B. henselae LPS and members of the Hbp family of proteins did not appear to stimulate an humoral response in any infected cats. Seven proteins were recognized by at least 70% of sera tested, but only three were recognized by all sera. Nanospray-tandem mass spectrometry was used to identify OM components, including the immunodominant OM proteins. Recognition of the nonimmunogenic nature of the major OM components, such as LPS, and identification of the predominant immunogens should elucidate the mechanisms by which B. henselae establishes persistent bacteremic infections within cats. Additionally, the common antigens may serve as potential feline vaccine candidates to eliminate the pathogen from its animal reservoir.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Predominant Outer Membrane Antigens of Bartonella henselae

Chenoweth

Greene

Krause³

et al. 2004

Infect Immun

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“…The 30-kDa protein of B. quintana (HbpA) shows a close homology (49% identity) to a 31-kDa protein (Pap31) of B. henselae (6). The sequence of the pap31 gene was already described by Bowers et al in 1998, but the protein was not further characterized (3).…”

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confidence: 99%

“…For Bartonella quintana, as many as eight different heminbinding proteins (HBPs) have been identified, including 30-, 42-, and 87-kDa proteins (6). The 30-kDa protein of B. quintana (HbpA) shows a close homology (49% identity) to a 31-kDa protein (Pap31) of B. henselae (6).…”

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confidence: 99%

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Hemin Binding, Functional Expression, and Complementation Analysis of Pap 31 fromBartonella henselae

et al. 2003

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Growth of Bartonella henselae is strongly heme dependent, and B. henselae is unable to synthesize heme itself. At least five outer membrane-associated proteins from B. henselae bind hemin, including the 31-kDa protein designated Pap31. The gene of this protein was heterologously expressed in Escherichia coli M15(pREP4) and detected with monoclonal antibodies in the outer membrane fraction. Complementation of the hemA-deficient mutant E. coli K-12 EB53 (aroB tsx malT hemA) with pap31 demonstrated that this protein is involved in heme acquisition and may be an important virulence factor in the pathogenesis of B. henselae.

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BartonellaandAfipia

Sander

2010

Topley &Amp; Wilson's Microbiology and Microbial Infections

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Hemin-Binding Surface Protein from Bartonella quintana

Cited by 57 publications

References 63 publications

Predominant Outer Membrane Antigens of Bartonella henselae

Predominant Outer Membrane Antigens of Bartonella henselae

Hemin Binding, Functional Expression, and Complementation Analysis of Pap 31 fromBartonella henselae

BartonellaandAfipia

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