Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C

Braun-Breton, Catherine; Rosenberry, Terrone L.; Silva, Luiz Pereira da

doi:10.1038/332457a0

Cited by 142 publications

(59 citation statements)

References 26 publications

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“…First, binding of AMA1 to erythrocytes requires the proteolytic cleavage of the erythrocyte. Previous data on P. chabaudi merozoites showed that diisopropylfluorophosphate-treated merozoites could not invade erythrocytes unless the erythrocytes were pretreated with ␣-chymotrypsin or proteases extracted from parasites (21). This observation suggests that the protease modifies the erythrocyte surface during invasion.…”

Section: Reduced Invasion Into Kxnull Erythrocytesmentioning

confidence: 67%

“…Thus, binding of domain III of AMA1 depends on trypsin treatment of erythrocytes for either exposure of the Kx binding site or cleavage of the Kx protein. It is known that a protease is required for invasion by merozoites of P. chabaudi into mouse erythrocytes (21). Could a trypsin-like protease be involved in the modification of human erythrocyte surface by P. falciparum during invasion?…”

Section: Enzyme Treatment Of Erythrocytes Modifies the Kx Proteinmentioning

confidence: 99%

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Domain III of Plasmodium falciparum apical membrane antigen 1 binds to the erythrocyte membrane protein Kx

Kato

Mayer

Singh

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Plasmodium falciparum apical membrane antigen 1 (AMA1) is located in the merozoite micronemes, an organelle that contains receptors for invasion, suggesting that AMA1 may play a role in this process. However, direct evidence that P. falciparum AMA1 binds to human erythrocytes is lacking. In this study, we determined that domain III of AMA1 binds to the erythrocyte membrane protein, Kx, and that the rate of invasion of Kx null erythrocytes is reduced, indicating a significant but not unique role of AMA1 and Kx in parasite invasion of erythrocytes. Domains I͞II͞III, domains I͞II and domain III of AMA1 were expressed on the surface of CHO-K1 cells, and their ability to bind erythrocytes was determined. We observed that each of these domains failed to bind untreated human erythrocytes. In contrast, domain III, but not the other domains of AMA1, bound to trypsin-treated human erythrocytes. We tested the binding of AMA1 to trypsin-treated genetically mutant human erythrocytes, missing various erythrocyte membrane proteins. AMA1 failed to bind trypsin-treated Kx null (McLeod) erythrocytes, which lack the Kx protein. Furthermore, treatmentofhumanerythrocyteswithtrypsin,followedby␣-chymotrypsin, cleaved Kx and destroyed the binding of AMA1 to human erythrocytes. Lastly, the rate of invasion of Kx null erythrocytes by P. falciparum was significantly lower than Kx-expressing erythrocytes. Taken together, our data suggest that AMA1 plays an important, but not exclusive, role in invasion of human erythrocytes through a process that involves exposure or modification of the erythrocyte surface protein, Kx, by a trypsin-like enzyme. T he complex multistep process of invasion of erythrocytes byPlasmodium falciparum begins with the binding of any surface of the merozoite, followed by reorientation to put the merozoite's apical end in close apposition to the erythrocyte surface. The apical end of merozoites contains the organelles of invasion, including the micronemes that contain receptors such as members of the Duffy binding protein family of erythrocytebinding ligands (1). A junction forms between P. knowlesi merozoites and the erythrocyte before the merozoite is brought into the erythrocyte. The junction only forms and invasion only occurs between P. knowlesi merozoites and Duffy blood group positive human erythrocytes. Duffy null cells fail to form a junction and are not invaded by P. knowlesi merozoites (2). However, trypsin-or neuraminidase-treated human Duffy null erythrocytes could form a junction and were invaded by P. knowlesi merozoites (3) despite the fact that untreated and trypsin-treated human Duffy null cells fail to bind any of the P. knowlesi Duffy binding proteins expressed on COS-7 cells (2). This result indicates that molecules other than the parasite Duffy binding protein family are exposed by enzyme treatment to form the junction between Duffy negative human erythrocytes and P. knowlesi merozoites. One of the possible junction-forming molecules is apical merozoite antigen 1 (AMA1), which is found in the mic...

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Section: Reduced Invasion Into Kxnull Erythrocytesmentioning

confidence: 67%

Section: Enzyme Treatment Of Erythrocytes Modifies the Kx Proteinmentioning

confidence: 99%

Domain III of Plasmodium falciparum apical membrane antigen 1 binds to the erythrocyte membrane protein Kx

Kato

Mayer

Singh

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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“…The existence of pro teolytic activity in the erythrocytic stages of Plasmodium is well described in the literature (Shrevel et al, 1990). These malaria proteases are divided in two groups, one active in an acidic envi ronment and involved in haemoglobin degradation (Bailly etal, 1991;Dame et al, 1994;Goldberg et al, 1991;Rosenthal etal, 1989;Vander Jagt etal, 1986), the other active in schizonts and/or merozoites with a role in merozoite maturation or red blood cell invasion (Banyal et al, 1990;Braun-Breton et al, 1988;Lyon et al, 1986;Rosenthal et al, 1987). The latter could also be involved in the regulation of parasite development within the hepatocyte.…”

Section: Discussionmentioning

confidence: 99%

Non specific resistance against malaria pre-erythrocytic stages: involvement of acute phase proteins

et al. 1995

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Summary :Levels of different acute phase proteins were compared in sera from parasitaemic and non-parasitaemic women living in a Plasmodium falciparum endemic area of Thailand. The ability of their sera to interfere with hepatic stage development of the para site was examined. Correlations were found between levels of α-1 antitrypsin, α-2 macroglobulin, hemopexin and the potential of sera to block hepatocyte invasion by the sporozoite.KEY WORDS : malaria, exo-erythrocytic stage, acute phase proteins.

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“…Antibodies raised against the two antigens do not cross-react (R. Ridley and U. Certa, unpublished observations). In addition, the 80 kDa component of the antigen defined by mAb Hb31cl 3 has been identified as a serine protease (BraunBreton, Rosenberry & Pereira da Silva, 1988). The gene sequence encoding RAP-1 has been cloned and sequenced and does not contain any of the motifs characteristic of serine proteases (Ridley et al 1990).…”

Section: Discussionmentioning

confidence: 99%

A rhoptry antigen ofPlasmodium falciparumis protective inSaimirimonkeys

Ridley¹,

Takács

Etlinger

et al. 1990

Parasitology

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SUMMARYA non-polymorphic antigen associated with the rhoptry organelles of Plasmodium falciparum has been purified by immunoaffinity chromatography. The antigen, RAP-1 (rhoptry associated protein-1), which is defined by monoclonal antibodies which inhibit parasite growth in vitro, is a multi-component antigen consisting of four major proteins of 80, 65, 42 and 40 kDa and two minor proteins of 77 and 70 kDa. These proteins were electro-eluted from preparative sodium dodecyl sulphate polyacrylamide gels and protected Saimiri sciureus monkeys from a lethal blood-stage infection of P. falciparum malaria. Sera from the protected animals recognized only proteins of the RAP-1 antigen when used to probe a Western blot of total parasite protein extract, confirming that RAP-1 is responsible for eliciting the protective immune response.

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Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C

Cited by 142 publications

References 26 publications

Domain III of Plasmodium falciparum apical membrane antigen 1 binds to the erythrocyte membrane protein Kx

Domain III of Plasmodium falciparum apical membrane antigen 1 binds to the erythrocyte membrane protein Kx

Non specific resistance against malaria pre-erythrocytic stages: involvement of acute phase proteins

A rhoptry antigen ofPlasmodium falciparumis protective inSaimirimonkeys

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