Acidic phosphoproteins associated with the host erythrocyte membrane of erythrocytes infected with Plasmodium berghei and P. chabaudi.

Abstract:

:New phosphoproteins appear on the host erythrocyte membrane during Plasmodium berghei and P. chabaudi infection. Distinct proteins having similar properties and all distinguished by isoelectric points of less than 4.0 are identified. Associated with the erythrocyte membranes of P. berghei infected erythrocytes are two proteins with molecular masses of 65 and 46 kDa, whereas 93, 90 and 76 kDa proteins are observed during P. chabaudi infection. These new erythrocyte membrane associated proteins are all of parasite origin as indicated by metabolic labeling with proline and are synthesized during the ring stage of the asexual replicative cycle. Three of these proteins, the 93 kDa P. chabaudi protein and both P. berghei proteins, have been purified and the amino acid composition determined. All three are characterized by a relatively high proportion of aspartate and glutamate residues. Mono-and polyclonal antibodies were also raised against the same three purified proteins. No cross reactivity between these three proteins is observed, but one monoclonal antibody against the 65 kDa P. berghei crossreacts with a 27 kDa mouse erythrocyte protein. Immunofluorescence using the antibodies in combination with subcellular fractionation studies clearly shows that these phosphoproteins are associated with the host erythrocyte membrane and not the parasite.

journal_name

Mol Biochem Parasitol

authors

Wiser MF,Leible MB,Plitt B

doi

10.1016/0166-6851(88)90020-5

subject

Has Abstract

pub_date

1988-01-01 00:00:00

pages

11-21

issue

1

eissn

0166-6851

issn

1872-9428

pii

0166-6851(88)90020-5

journal_volume

27

pub_type

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