Abstract
Endotoxic lipopolysaccharide (LPS), a common structural component of all gram-negative bacteria, is well recognized for its capacity to interact with and perturb immunologically relevant cells. Using a radioiodinated, photoactivatable LPS probe, we have recently identified an 80-kilodalton LPS-specific binding protein on murine B lymphocytes. We now have extended these studies to determine if other mammalian species, as well as representative endotoxin-resistant species (frog and chicken), have a similar LPS-binding protein. We have identified what appears to be a relatively conserved 80-kilodalton LPS-binding protein on mononuclear cells of all mammalian species tested. However, both frog and chicken leukocytes failed to show the presence of a similar LPS-binding protein. It is possible that the presence of specific LPS-binding proteins may be important for endotoxin sensitivity of most mammalian species.
MeSH Terms
Animals
Carrier Proteins/analysis
Cattle
Chickens
Dogs
Endotoxins/metabolism,pharmacology
Goats
Horses
Lipopolysaccharides/metabolism
Lymphocytes/drug effects,metabolism
Mice
Molecular Weight
Rabbits
Rana catesbeiana
Sheep
Species Specificity
Swine
Chemicals
Carrier Proteins
Endotoxins
Lipopolysaccharides
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Roeder D J
Department of Microbiology, University of Kansas Medical Center 66103.
Lei M G
Morrison D C
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