Treponema pallidum rare outer membrane proteins

Analysis of mobility by freeze-fracture electron microscopy

K. W. Bourell, W. Schulz, M. V. Norgard, J. D. Radolf

Research output: Contribution to journalArticle

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Abstract

Freeze-fracture and deep-etch electron microscopy were used to investigate the molecular architecture of the Treponema pallidum outer membrane (OM). Freeze-fracture electron microscopy of treponemes freshly harvested from rabbit testes revealed that the intramembranous particles (IMPs) in both the concave and convex OM leaflets were distributed into alternating areas of relatively high and low particle density; in many OM fractures, IMPs formed rows that ran either parallel to or obliquely across the fracture faces. Statistical analysis (runs test) confirmed that the IMPs were nonrandomly distributed in both OM leaflets. Examination of deep-etched specimens revealed that the particles observed in freeze-fractured OMs also were surface exposed. Combined analysis of deep-etched and cross-fractured treponemes revealed that the OM particles were located in regions of the OM away from the endoflagella and closely apposed to the cytoplasmic membrane- peptidoglycan complex. When treponemes were incubated for extended periods with heat-inactivated immune rabbit syphilitic serum, no alteration in the distribution of OM IMPs was detected. In further experiments, approximately 1:1 mixtures of T. pallidum and Escherichia coli or separate suspensions of the nonpathogenic Treponema phagedenis biotype Reiter were fixed at 34°C or after cooling to 0°C (to induce lateral phase separation that would aggregate IMPs). Only particles in the T. pallidum OM failed to aggregate in cells fixed at the lower temperature. The combined data suggest that the mobility of T. pallidum rare OM proteins is limited, perhaps as a result of interactions between their periplasmic domains and components of the peptidoglycan-cytoplasmic membrane complex.

Original languageEnglish (US)
Pages (from-to)1598-1608
Number of pages11
JournalJournal of Bacteriology
Volume176
Issue number6
StatePublished - 1994

Fingerprint

Treponema pallidum
Electron Microscopy
Membrane Proteins
Membranes
Peptidoglycan
Cell Membrane
Treponema
Rabbits
Testis
Suspensions
Hot Temperature
Escherichia coli
Temperature

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

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Treponema pallidum rare outer membrane proteins : Analysis of mobility by freeze-fracture electron microscopy. / Bourell, K. W.; Schulz, W.; Norgard, M. V.; Radolf, J. D.

In: Journal of Bacteriology, Vol. 176, No. 6, 1994, p. 1598-1608.

Research output: Contribution to journalArticle

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