J Bacteriol Virol.  2004 Dec;34(4):283-289.

The Attachment of Detergent-Extracted Outer Membrane Proteins of Orientia tsutsugamushi to the Host Cell Surface

• Kim MK
• Kim MJ
• Lim BU
• Kang JS

Abstract

Orientia tsutsugamushi, a causative agent of scrub typhus, is an obligate intracellular parasite. The mechanisms by which O. tsutsugamushi invade host cells are unknown. Given the importance of surface-exposed proteins in the pathogenesis of microbial pathogens, outer membrane proteins (OMP) of O. tsutsugamushi were extracted with detergents and their cellular binding was studied. Outer membrane fraction of O. tsutsugamushi was enriched by a sodium-lauryl sarcosinate (Sarkosyl) treatment of total membranes. Outer membrane proteins were extracted by the treatment with sodium dodecyl sulfate (SDS) and Sarkosyl. The resulting soluble fractions were examined for their cellular binding by the immunofluorescence microscopy. A fifty six kilodalton protein was found to bind to fixed ECV304 cells only when the outer membrane preparation was not treated by DTT or heat. These results suggest that the conformation the 56-kDa OMP is important for the attachment to the host cell surfaces.

Keyword

Orientia tsutsugamushi; Outer membrane protein; 56-kDa protein

MeSH Terms

Detergents
Hot Temperature
Membrane Proteins*
Membranes*
Microscopy, Fluorescence
Orientia tsutsugamushi*
Parasites
Scrub Typhus
Sodium Dodecyl Sulfate
Detergents
Membrane Proteins
Sodium Dodecyl Sulfate