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PMID: 806524 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Adsorption of typhus rickettsiae to ghosts of sheep erythrocytes.

Infection and immunity ·Vol. 11 ·No. 6 ·1975-06-00 ·Pages 1244-51

Winkler HH, Ramm LE

Abstract

Rickettsia prowazeki will adsorb to ghosts derived from sheep erythrocytes by hypotonic lysis. Adsorption to ghosts, as to intact erythrocytes, is dependent on the metabolism of the rickettsiae. KCN and 0 C inhibit adsorption. Fluoride, while inhibiting hemolysis, has no effect on adsorption to ghosts or intact erythrocytes. The adsorption of rickettsiae to ghosts does not lead to lysis, in that fluorescent albumin can be retained by the ghost after adsorption. Both inside-out and right-side-out vesicles formed from the ghost are equally capable of adsorption, indicating that the receptor is stable during the process of vesiculation and is not localized to one aspect of the cell membrane. Adsorption to ghosts is slower and displays less affinity than to the intact erythrocyte. The ghost system will be useful in characterizing the membrane receptor for rickettsia and in establishing assays for adsorption to other cells.

MeSH Terms
Adsorption Animals Binding Sites Cell Membrane/immunology Erythrocytes/immunology Fluorescent Antibody Technique Hemolysis Rickettsia prowazekii/immunology Serum Albumin, Bovine Sheep Sialic Acids/analysis Time Factors
Chemicals
Sialic Acids Serum Albumin, Bovine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Winkler H H
Ramm L E
References (10)
10 references, click to expand
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
1975-06-00
Pages
1244-51
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC415206
Subset
IM
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