An exported protein of Plasmodium falciparum is synthesized as an integral membrane protein
Exp-1 is an antigen of Plasmodium falciparum which is transported from the parasite cell to the membrane of the parasitophorous vacuole and to membranous compartments in the erythrocyte. To investigate how this protein is transported, we studied the synthesis and membrane translocation of exp-1 in a...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1991-05, Vol.46 (1), p.149-157 |
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| container_title | Molecular and biochemical parasitology |
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| creator | Günther, Kathrin Tümmler, Meike Arnold, Hans-Henning Ridley, Robert Goman, Michael Scaife, John G. Lingelbach, Klaus |
| description | Exp-1 is an antigen of
Plasmodium falciparum which is transported from the parasite cell to the membrane of the parasitophorous vacuole and to membranous compartments in the erythrocyte. To investigate how this protein is transported, we studied the synthesis and membrane translocation of exp-1 in a cell-free system. The protein was translocated into canine pancreatic microsomes. Its N-terminal half was thus protected from proteinase K digestion, suggesting that exp-1 is an integral membrane protein with its N-terminus facing the lumen of the microsomes. This conclusion has been confirmed in vivo. In parasitized erythrocytes, exp-1 is membrane-associated and resistant to extraction with alkali, as would be expected for an integral membrane protein. Moreover, using segment-specific monoclonal antibodies, we have shown that here again the N-terminus of exp-1 faces the inside of vesicles, inaccessible to proteases, whereas the C-terminus is degraded. We conclude that exp-1 is an integral membrane protein and infer that it is transported by vesicles from the parasite to a compartment in the host cell cytoplasm. |
| doi_str_mv | 10.1016/0166-6851(91)90208-N |
| format | Article |
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Plasmodium falciparum which is transported from the parasite cell to the membrane of the parasitophorous vacuole and to membranous compartments in the erythrocyte. To investigate how this protein is transported, we studied the synthesis and membrane translocation of exp-1 in a cell-free system. The protein was translocated into canine pancreatic microsomes. Its N-terminal half was thus protected from proteinase K digestion, suggesting that exp-1 is an integral membrane protein with its N-terminus facing the lumen of the microsomes. This conclusion has been confirmed in vivo. In parasitized erythrocytes, exp-1 is membrane-associated and resistant to extraction with alkali, as would be expected for an integral membrane protein. Moreover, using segment-specific monoclonal antibodies, we have shown that here again the N-terminus of exp-1 faces the inside of vesicles, inaccessible to proteases, whereas the C-terminus is degraded. We conclude that exp-1 is an integral membrane protein and infer that it is transported by vesicles from the parasite to a compartment in the host cell cytoplasm.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/0166-6851(91)90208-N</identifier><identifier>PMID: 1852170</identifier><identifier>CODEN: MBIPDP</identifier><language>eng</language><publisher>Shannon: Elsevier B.V</publisher><subject>Animals ; Antigens, Protozoan - biosynthesis ; Antigens, Protozoan - genetics ; Antigens, Protozoan - metabolism ; Antigens, Surface - biosynthesis ; Antigens, Surface - metabolism ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; Biological Transport, Active ; Cell-Free System ; Chickens ; Cloning, Molecular ; Dogs ; Fundamental and applied biological sciences. Psychology ; Intracellular transport ; Malaria - parasitology ; Membrane protein ; Microsomes - metabolism ; Muramidase - metabolism ; Pancreas - metabolism ; Plasmodium falciparum ; Plasmodium falciparum - metabolism ; Protein Precursors - metabolism ; Protein Processing, Post-Translational ; Protozoa ; Secretion ; Segment-specific antibodies</subject><ispartof>Molecular and biochemical parasitology, 1991-05, Vol.46 (1), p.149-157</ispartof><rights>1991</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-5586723394704377bed10d83ce7742bf5d13b4e4416c5192a4dcea6adf293c23</citedby><cites>FETCH-LOGICAL-c386t-5586723394704377bed10d83ce7742bf5d13b4e4416c5192a4dcea6adf293c23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0166-6851(91)90208-N$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5044784$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1852170$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Günther, Kathrin</creatorcontrib><creatorcontrib>Tümmler, Meike</creatorcontrib><creatorcontrib>Arnold, Hans-Henning</creatorcontrib><creatorcontrib>Ridley, Robert</creatorcontrib><creatorcontrib>Goman, Michael</creatorcontrib><creatorcontrib>Scaife, John G.</creatorcontrib><creatorcontrib>Lingelbach, Klaus</creatorcontrib><title>An exported protein of Plasmodium falciparum is synthesized as an integral membrane protein</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>Exp-1 is an antigen of
Plasmodium falciparum which is transported from the parasite cell to the membrane of the parasitophorous vacuole and to membranous compartments in the erythrocyte. To investigate how this protein is transported, we studied the synthesis and membrane translocation of exp-1 in a cell-free system. The protein was translocated into canine pancreatic microsomes. Its N-terminal half was thus protected from proteinase K digestion, suggesting that exp-1 is an integral membrane protein with its N-terminus facing the lumen of the microsomes. This conclusion has been confirmed in vivo. In parasitized erythrocytes, exp-1 is membrane-associated and resistant to extraction with alkali, as would be expected for an integral membrane protein. Moreover, using segment-specific monoclonal antibodies, we have shown that here again the N-terminus of exp-1 faces the inside of vesicles, inaccessible to proteases, whereas the C-terminus is degraded. We conclude that exp-1 is an integral membrane protein and infer that it is transported by vesicles from the parasite to a compartment in the host cell cytoplasm.</description><subject>Animals</subject><subject>Antigens, Protozoan - biosynthesis</subject><subject>Antigens, Protozoan - genetics</subject><subject>Antigens, Protozoan - metabolism</subject><subject>Antigens, Surface - biosynthesis</subject><subject>Antigens, Surface - metabolism</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>Biological Transport, Active</subject><subject>Cell-Free System</subject><subject>Chickens</subject><subject>Cloning, Molecular</subject><subject>Dogs</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Intracellular transport</subject><subject>Malaria - parasitology</subject><subject>Membrane protein</subject><subject>Microsomes - metabolism</subject><subject>Muramidase - metabolism</subject><subject>Pancreas - metabolism</subject><subject>Plasmodium falciparum</subject><subject>Plasmodium falciparum - metabolism</subject><subject>Protein Precursors - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Protozoa</subject><subject>Secretion</subject><subject>Segment-specific antibodies</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoMotVb_gUIOInpYTbLZJHsRpPgFoh68eQjZZFYj-1GTrVh_vSmtehMSEphn3hkehPYpOaWEirN0RSZUQY9LelISRlR2v4HGVEmWlZypTTT-RbbRToxvhJBCCjFCI6oKRiUZo-eLDsPnrA8DODwL_QC-w32NHxsT2975eYtr01g_MyF9fcRx0Q2vEP1X4k3EpsO-G-AlmAa30FbBdPCTs4u2Um-EvfU7QU9Xl0_Tm-zu4fp2enGX2VyJISsKJSTL85JLwnMpK3CUOJVbkJKzqi4czSsOnFNhC1oyw50FI4yrWZlblk_Q0So2jX2fQxx066OFpkmr9POoFRGqpFQkkK9AG_oYA9R6FnxrwkJTopdK9dKXXvrSZTpLpfo-tR2s8-dVC-6vaeUw1Q_XdROtaeqkwPr4ixWEc6l4ws5XGCQVHx6CjtZDZ8H5AHbQrvf_7_ENVRiSxA</recordid><startdate>19910501</startdate><enddate>19910501</enddate><creator>Günther, Kathrin</creator><creator>Tümmler, Meike</creator><creator>Arnold, Hans-Henning</creator><creator>Ridley, Robert</creator><creator>Goman, Michael</creator><creator>Scaife, John G.</creator><creator>Lingelbach, Klaus</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19910501</creationdate><title>An exported protein of Plasmodium falciparum is synthesized as an integral membrane protein</title><author>Günther, Kathrin ; Tümmler, Meike ; Arnold, Hans-Henning ; Ridley, Robert ; Goman, Michael ; Scaife, John G. ; Lingelbach, Klaus</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-5586723394704377bed10d83ce7742bf5d13b4e4416c5192a4dcea6adf293c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Animals</topic><topic>Antigens, Protozoan - biosynthesis</topic><topic>Antigens, Protozoan - genetics</topic><topic>Antigens, Protozoan - metabolism</topic><topic>Antigens, Surface - biosynthesis</topic><topic>Antigens, Surface - metabolism</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>Biological Transport, Active</topic><topic>Cell-Free System</topic><topic>Chickens</topic><topic>Cloning, Molecular</topic><topic>Dogs</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Intracellular transport</topic><topic>Malaria - parasitology</topic><topic>Membrane protein</topic><topic>Microsomes - metabolism</topic><topic>Muramidase - metabolism</topic><topic>Pancreas - metabolism</topic><topic>Plasmodium falciparum</topic><topic>Plasmodium falciparum - metabolism</topic><topic>Protein Precursors - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Protozoa</topic><topic>Secretion</topic><topic>Segment-specific antibodies</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Günther, Kathrin</creatorcontrib><creatorcontrib>Tümmler, Meike</creatorcontrib><creatorcontrib>Arnold, Hans-Henning</creatorcontrib><creatorcontrib>Ridley, Robert</creatorcontrib><creatorcontrib>Goman, Michael</creatorcontrib><creatorcontrib>Scaife, John G.</creatorcontrib><creatorcontrib>Lingelbach, Klaus</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Günther, Kathrin</au><au>Tümmler, Meike</au><au>Arnold, Hans-Henning</au><au>Ridley, Robert</au><au>Goman, Michael</au><au>Scaife, John G.</au><au>Lingelbach, Klaus</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An exported protein of Plasmodium falciparum is synthesized as an integral membrane protein</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1991-05-01</date><risdate>1991</risdate><volume>46</volume><issue>1</issue><spage>149</spage><epage>157</epage><pages>149-157</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><coden>MBIPDP</coden><abstract>Exp-1 is an antigen of
Plasmodium falciparum which is transported from the parasite cell to the membrane of the parasitophorous vacuole and to membranous compartments in the erythrocyte. To investigate how this protein is transported, we studied the synthesis and membrane translocation of exp-1 in a cell-free system. The protein was translocated into canine pancreatic microsomes. Its N-terminal half was thus protected from proteinase K digestion, suggesting that exp-1 is an integral membrane protein with its N-terminus facing the lumen of the microsomes. This conclusion has been confirmed in vivo. In parasitized erythrocytes, exp-1 is membrane-associated and resistant to extraction with alkali, as would be expected for an integral membrane protein. Moreover, using segment-specific monoclonal antibodies, we have shown that here again the N-terminus of exp-1 faces the inside of vesicles, inaccessible to proteases, whereas the C-terminus is degraded. We conclude that exp-1 is an integral membrane protein and infer that it is transported by vesicles from the parasite to a compartment in the host cell cytoplasm.</abstract><cop>Shannon</cop><pub>Elsevier B.V</pub><pmid>1852170</pmid><doi>10.1016/0166-6851(91)90208-N</doi><tpages>9</tpages></addata></record> |
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| ispartof | Molecular and biochemical parasitology, 1991-05, Vol.46 (1), p.149-157 |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals Antigens, Protozoan - biosynthesis Antigens, Protozoan - genetics Antigens, Protozoan - metabolism Antigens, Surface - biosynthesis Antigens, Surface - metabolism Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Biological Transport, Active Cell-Free System Chickens Cloning, Molecular Dogs Fundamental and applied biological sciences. Psychology Intracellular transport Malaria - parasitology Membrane protein Microsomes - metabolism Muramidase - metabolism Pancreas - metabolism Plasmodium falciparum Plasmodium falciparum - metabolism Protein Precursors - metabolism Protein Processing, Post-Translational Protozoa Secretion Segment-specific antibodies |
| title | An exported protein of Plasmodium falciparum is synthesized as an integral membrane protein |
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