Recognition and invasion of human erythrocytes by malarial parasites: contribution of sialoglycoproteins to attachment and host specificity
The receptivity of human erythrocytes to invasion by Plasmodium falciparum merozoites can be decreased by neuraminidase or trypsin treatment, an observation that supports a role for the erythrocyte sialoglycoproteins (glycophorins) in invasion. We have found that ..cap alpha../sub 1/-acid glycoprotein (AGP), added to in vitro cultures, can restore invasion of enzyme-treated human erythrocytes. AGP is structurally different from the glycophorins although it does carry 12% sialic acid. Its ability to restore receptivity to desialylated cells is dependent on its sialic acid complement, its concentration, and its binding to the erythrocyte surface. We present evidence that AGP forms a bridge between the merozoite and the enzyme-treated erythrocyte that allows the stronger and more complex interactions of invasion to proceed. We suggest that the glycophorins play the same role on the surface of the intact erythrocyte. 31 references, 3 figures, 6 tables.
- Research Organization:
- Univ. of California, San Francisco, CA (United States)
- DOE Contract Number:
- AC03-76SF00098
- OSTI ID:
- 5751956
- Journal Information:
- J. Cell Biol.; (United States), Vol. 98:5
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
GLUCOPROTEINS
CHEMICAL BONDS
MOLECULAR STRUCTURE
MALARIA
PATHOGENESIS
BIOCHEMISTRY
ENZYME ACTIVITY
ERYTHROCYTES
HOST
MAN
O-GLYCOSYL HYDROLASES
RECEPTORS
TRYPSIN
ANIMALS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARBOHYDRATES
CHEMISTRY
DISEASES
ENZYMES
GLYCOSYL HYDROLASES
HYDROLASES
INFECTIOUS DISEASES
MAMMALS
MATERIALS
ORGANIC COMPOUNDS
PARASITIC DISEASES
PEPTIDE HYDROLASES
PRIMATES
PROTEINS
SACCHARIDES
SERINE PROTEINASES
VERTEBRATES
550900* - Pathology