Abstract
Two apparent isoforms of the virulence-associated 69,000-molecular-weight protein pertactin were purified from Bordetella pertussis. Mass spectrometry showed a difference of 2,060 Da, which may result from differential C-terminal cleavage of a larger precursor. Both forms were protective in a mouse model, eliciting bactericidal antibodies and reducing respiratory tract colonization.
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal / immunology
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Antigens, Bacterial / chemistry
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Bacterial Outer Membrane Proteins / chemistry*
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Bacterial Outer Membrane Proteins / immunology
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Bacterial Vaccines / immunology
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Blotting, Western
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Bordetella pertussis / chemistry*
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Bordetella pertussis / immunology
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Immunization
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Mass Spectrometry
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Mice
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Molecular Sequence Data
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Molecular Weight
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Virulence Factors, Bordetella*
Substances
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Antibodies, Monoclonal
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Antigens, Bacterial
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Bacterial Outer Membrane Proteins
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Bacterial Vaccines
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Virulence Factors, Bordetella
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pertactin