Leucocytosis-Promoting Factor of
            <i>Bordetella pertussis</i>
            I. Purification and Characterization

Sato, Yuji; Arai, Hideo

doi:10.1128/iai.6.6.899-904.1972

Cited by 55 publications

(33 citation statements)

References 19 publications

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“…Differential centrifugation strongly suggested that the hemagglutinating properties did reside in the filamentous particles. These results are consistent with the findings of Sato and his colleagues (26)(27)(28) but they also suggested that the filaments were identical with LPF and HSF, an observation that is not confirmed by the present studies. They also proposed that the filaments can induce protection against experimental pertussis, an observation which preliminary results in our laboratory tend to verify.…”

Section: Phase I Cells Of B Pertussis and Their Products Induce A Nusupporting

confidence: 89%

“…pertuss/s which had LPF as well as HSF activity and which contained greater than 50% lipid (16). In their filament-rich preparations with LPF activity Sate and Arai (26) also reported the presence of 17.5% lipid, and Munoz and Hestekin (31) found 28.4% lipid in partially purified HSF, but in these cases the products were clearly heterogenous.…”

Section: Phase I Cells Of B Pertussis and Their Products Induce A Numentioning

confidence: 94%

See 1 more Smart Citation

Isolation and properties of the leukocytosis- and lymphocytosis-promoting factor of Bordetella pertussis.

Morse¹,

Morse²

1976

The Journal of Experimental Medicine

166

105

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In a previous report on the effects of the leukocytosis-and lymphocytosispromoting factor (LPF) 1 ofBordetella pertussis on cyclic adenosine 3':5'-monophosphate (cAMP) metabolism, a method for isolation of highly active LPF was presented briefly (1). In the present communication, the results of further studies on the isolation and chemical, immunochemical, and biological properties of LPF are described. It has been found that a single moiety is responsible for the induction in mice of leukocytosis with both lymphocytosis and granulocytosis, histamine sensitization, and hypoglycemia and unresponsiveness to the hyperglycemic effects of epinephrine. In confirmation of our preliminary report (2), LPF has been found to be clearly distinct from the hemagglutinating pili of B. pertussis, the properties of which are also described. Materials and MethodsB. pertussis Cultures. Strain NIH 114 (3779B), which has been utilized in continuing studies in this laboratory was also employed in the present investigations. Lyophilizod samples, obtained through the courtesy of Dr. Charles Manclark, Bureau of Biologics, Bethesda, Md., were reconstituted in sterile distilled H~O and plated on Bordet-Gengou medium (Clinical Sciences Inc., Whippany, N. J.). The 2-day growth at 36°C on one Petri dish was harvested in 10 ml of 2% casamino acids (technical grade; Difco Laboratories, Detroit, Mich.), and 1 ml of the suspension was inoculated into 100 ml of liquid medium in i liter Blake bottles. After 2 days of incubation at 36°C, 10 ml of the seed culture (approximately 5 × 10 x° organJma) was inoculated into 1 liter of liquid medium in Povitsky bottles which were then incubated at 35-36°C. In order to provide maximum surface area for aeration, all bottles were placed in the horizontal position during incubation. In the case of the 100 ml cultures, the depth of the medium was 1.0 cm and the surface area 218 cm2; the values for the 1-1iter cultures were 2.5 cm and 580 cm 2, respectively.The liquid medium was that previously described (3) except for the omission of an anion exchange resin which was found to be unnecessary for either optimal growth, maintenance of the Phase I state, or maximal production of LPF. Culture density was assessed with the National Institutes of Health opacity standard, and the criteria utilized to determine whether the organisms were Phase I included: a homogenous population of small, gram-negative coccobacilli and

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Section: Phase I Cells Of B Pertussis and Their Products Induce A Nusupporting

confidence: 89%

Section: Phase I Cells Of B Pertussis and Their Products Induce A Numentioning

confidence: 94%

Isolation and properties of the leukocytosis- and lymphocytosis-promoting factor of Bordetella pertussis.

Morse¹,

Morse²

1976

The Journal of Experimental Medicine

166

105

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“…Arai and Sato (3) called these fimbrial HA (FHA) and leukocytosis-promoting factor HA. These substances were separated from leukocytosis-promoting factor preparations previously thought to be pure (28)(29)(30). Arai and Sato (3) and Sato et al (31) showed that FHA was nontoxic and protected mice from i.c.…”

mentioning

confidence: 99%

Mouse-protecting and histamine-sensitizing activities of pertussigen and fimbrial hemagglutinin from Bordetella pertussis

Muñoz¹,

Arai²,

Cole³

1981

Infect Immun

126

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We compared the protective activities of fimbrial hemagglutinin (FHA) and pertussigen and their respective antibodies in mice infected intracerebrally with Bordetellapertussis. We found that mice were protected by a 1.7-/ug/mouse dose of pertussigen which was free of detectable FHA and was detoxified by treatment with glutaraldehyde. A pertussigen preparation made from cells grown in shake cultures that did not contain demonstrable FHA protected mice at a dose of 1.4

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“…The bacterial strains used In this work were: S. perfuss/'s Tohama, 1.2 serotype (Sato and Arai. 1972); B. pertussis H36 1.3 serotype and B. parapertussis M/S180, N. Preston; E. co// DH5, end1A^.…”

Section: Bacterial Strains Piasmids and Mediamentioning

confidence: 99%

Engineering upstream transcriptional and translational signals of Bordetella pertussis serotype 2 fimbrial subunit protein for efficient expression in Escherichia coli: in vitro autoassembly of the expressed product into filamentous structures

Walker

Rohde

Brownlie

et al. 1990

Molecular Microbiology

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Escherichia coli containing a cloned gene encoding the Bordetella pertussis serotype 2 fimbrial subunit failed to produce detectable levels of the gene product in whole-cell extracts. To engineer plasmids capable of directing the expression in E. coli of high levels of this product, both as a pre-protein and as a methionylated mature form the upstream signals of the fimbrial subunit gene were replaced by the lambda P(L) and P(R) promoters and the E. coli atpE translational initiation region. These constructs did not result in the expression of fimbrial subunit at detectable levels in several E. coli strains including DH5. However, they did in E. coli CAG629, which is lon protease and heat shock protein deficient. Both pre-protein and methionylated mature protein had molecular weights of 25.0 kD, which indicated that correct processing of the leader sequence had occurred and thus that it was transposed across the inner membrane. Electron microscopic investigation of the cell surface of E. coli cells expressing either form of the fimbrial gene failed to detect the presence of filamentous structures. The methionylated mature form of the recombinant fimbrial subunit was purified to apparent homogeneity. After dialysis in appropriate conditions it was seen to autoassemble into protein polymers. Antibodies raised against polymerized recombinant subunit reacted weakly with whole B. pertussis serotype 2 fimbriae in immunodot blot assays. However, such antibodies reacted in Western blots equally well with the recombinant and wild-type form of the fimbrial subunit.(ABSTRACT TRUNCATED AT 250 WORDS)

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Leucocytosis-Promoting Factor of Bordetella pertussis I. Purification and Characterization

Cited by 55 publications

References 19 publications

Isolation and properties of the leukocytosis- and lymphocytosis-promoting factor of Bordetella pertussis.

Isolation and properties of the leukocytosis- and lymphocytosis-promoting factor of Bordetella pertussis.

Mouse-protecting and histamine-sensitizing activities of pertussigen and fimbrial hemagglutinin from Bordetella pertussis

Engineering upstream transcriptional and translational signals of Bordetella pertussis serotype 2 fimbrial subunit protein for efficient expression in Escherichia coli: in vitro autoassembly of the expressed product into filamentous structures

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