Heat-modifiable envelope proteins of Bordetella pertussis

S. K. Armstrong, C. D. Parker

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Several envelope proteins of Bordetella pertussis demonstrated differences in electrophoretic mobility, depending upon solubilization temperature before sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These proteins were exposed on the cell surface as judged by their accessibility to radiolabeling with 125I. Monoclonal antibodies to two of the heat-modifiable proteins (M(r)s of 18,000 and 91,000) reacted with intact cells in immunofluorescence microscopy experiments, also indicating surface exposure of these two proteins. Two-dimensional gel electrophoresis revealed that two heat-modifiable proteins (a major protein with an M(r) of 38,000 and one with an M(r) of 18,000) migrated as higher-M(r) moieties when solubilized at low temperatures (25°C). Three proteins (M(r)s of 91,000, 32,000, and 30,000) and possibly a fourth (31,000) migrated as lower-M(r) species when solubilized at 25°C, as revealed in the two-dimensional gel system; these three proteins were found only in virulent B. pertussis and were not detected in a phase IV avirulent strain nor in a strain modulated to phenotypic avirulence by growth in nicotinic acid. The 38,000 molecular-weight protein (38K protein) and a 25K protein were found to be noncovalently associated with the underlying peptidoglycan. Small amounts of the 91K and 18K proteins were also found associated with peptidoglycan.

Original languageEnglish (US)
Pages (from-to)109-117
Number of pages9
JournalInfection and immunity
Volume54
Issue number1
DOIs
StatePublished - 1986

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