Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax

Publication Date:
2018-01-05
Publisher:
American Association for the Advancement of Science (AAAS)
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
Chemistry and Pharmacology
Geosciences
Computer Science
Medicine
Natural Sciences in General
Physics
Keywords:
Microbiology
Published by:
http://www.aaas.org/
_version_ 1836398735150546944
autor Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
beschreibung Plasmodium vivax shows a strict host tropism for reticulocytes. We identified transferrin receptor 1 (TfR1) as the receptor for P. vivax reticulocyte-binding protein 2b (PvRBP2b). We determined the structure of the N-terminal domain of PvRBP2b involved in red blood cell binding, elucidating the molecular basis for TfR1 recognition. We validated TfR1 as the biological target of PvRBP2b engagement by means of TfR1 expression knockdown analysis. TfR1 mutant cells deficient in PvRBP2b binding were refractory to invasion of P. vivax but not to invasion of P. falciparum . Using Brazilian and Thai clinical isolates, we show that PvRBP2b monoclonal antibodies that inhibit reticulocyte binding also block P. vivax entry into reticulocytes. These data show that TfR1-PvRBP2b invasion pathway is critical for the recognition of reticulocytes during P. vivax invasion.
citation_standardnr 6130867
datenlieferant ipn_articles
feed_id 25
feed_publisher American Association for the Advancement of Science (AAAS)
feed_publisher_url http://www.aaas.org/
insertion_date 2018-01-05
journaleissn 1095-9203
journalissn 0036-8075
publikationsjahr_anzeige 2018
publikationsjahr_facette 2018
publikationsjahr_intervall 7984:2015-2019
publikationsjahr_sort 2018
publisher American Association for the Advancement of Science (AAAS)
quelle Science
relation http://science.sciencemag.org/cgi/content/short/359/6371/48?rss=1
schlagwort Microbiology
search_space articles
shingle_author_1 Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
shingle_author_2 Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
shingle_author_3 Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
shingle_author_4 Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
shingle_catch_all_1 Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
Microbiology
Plasmodium vivax shows a strict host tropism for reticulocytes. We identified transferrin receptor 1 (TfR1) as the receptor for P. vivax reticulocyte-binding protein 2b (PvRBP2b). We determined the structure of the N-terminal domain of PvRBP2b involved in red blood cell binding, elucidating the molecular basis for TfR1 recognition. We validated TfR1 as the biological target of PvRBP2b engagement by means of TfR1 expression knockdown analysis. TfR1 mutant cells deficient in PvRBP2b binding were refractory to invasion of P. vivax but not to invasion of P. falciparum . Using Brazilian and Thai clinical isolates, we show that PvRBP2b monoclonal antibodies that inhibit reticulocyte binding also block P. vivax entry into reticulocytes. These data show that TfR1-PvRBP2b invasion pathway is critical for the recognition of reticulocytes during P. vivax invasion.
Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
American Association for the Advancement of Science (AAAS)
0036-8075
00368075
1095-9203
10959203
shingle_catch_all_2 Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
Microbiology
Plasmodium vivax shows a strict host tropism for reticulocytes. We identified transferrin receptor 1 (TfR1) as the receptor for P. vivax reticulocyte-binding protein 2b (PvRBP2b). We determined the structure of the N-terminal domain of PvRBP2b involved in red blood cell binding, elucidating the molecular basis for TfR1 recognition. We validated TfR1 as the biological target of PvRBP2b engagement by means of TfR1 expression knockdown analysis. TfR1 mutant cells deficient in PvRBP2b binding were refractory to invasion of P. vivax but not to invasion of P. falciparum . Using Brazilian and Thai clinical isolates, we show that PvRBP2b monoclonal antibodies that inhibit reticulocyte binding also block P. vivax entry into reticulocytes. These data show that TfR1-PvRBP2b invasion pathway is critical for the recognition of reticulocytes during P. vivax invasion.
Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
American Association for the Advancement of Science (AAAS)
0036-8075
00368075
1095-9203
10959203
shingle_catch_all_3 Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
Microbiology
Plasmodium vivax shows a strict host tropism for reticulocytes. We identified transferrin receptor 1 (TfR1) as the receptor for P. vivax reticulocyte-binding protein 2b (PvRBP2b). We determined the structure of the N-terminal domain of PvRBP2b involved in red blood cell binding, elucidating the molecular basis for TfR1 recognition. We validated TfR1 as the biological target of PvRBP2b engagement by means of TfR1 expression knockdown analysis. TfR1 mutant cells deficient in PvRBP2b binding were refractory to invasion of P. vivax but not to invasion of P. falciparum . Using Brazilian and Thai clinical isolates, we show that PvRBP2b monoclonal antibodies that inhibit reticulocyte binding also block P. vivax entry into reticulocytes. These data show that TfR1-PvRBP2b invasion pathway is critical for the recognition of reticulocytes during P. vivax invasion.
Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
American Association for the Advancement of Science (AAAS)
0036-8075
00368075
1095-9203
10959203
shingle_catch_all_4 Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
Microbiology
Plasmodium vivax shows a strict host tropism for reticulocytes. We identified transferrin receptor 1 (TfR1) as the receptor for P. vivax reticulocyte-binding protein 2b (PvRBP2b). We determined the structure of the N-terminal domain of PvRBP2b involved in red blood cell binding, elucidating the molecular basis for TfR1 recognition. We validated TfR1 as the biological target of PvRBP2b engagement by means of TfR1 expression knockdown analysis. TfR1 mutant cells deficient in PvRBP2b binding were refractory to invasion of P. vivax but not to invasion of P. falciparum . Using Brazilian and Thai clinical isolates, we show that PvRBP2b monoclonal antibodies that inhibit reticulocyte binding also block P. vivax entry into reticulocytes. These data show that TfR1-PvRBP2b invasion pathway is critical for the recognition of reticulocytes during P. vivax invasion.
Gruszczyk, J., Kanjee, U., Chan, L.-J., Menant, S., Malleret, B., Lim, N. T. Y., Schmidt, C. Q., Mok, Y.-F., Lin, K.-M., Pearson, R. D., Rangel, G., Smith, B. J., Call, M. J., Weekes, M. P., Griffin, M. D. W., Murphy, J. M., Abraham, J., Sriprawat, K., Menezes, M. J., Ferreira, M. U., Russell, B., Renia, L., Duraisingh, M. T., Tham, W.-H.
American Association for the Advancement of Science (AAAS)
0036-8075
00368075
1095-9203
10959203
shingle_title_1 Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
shingle_title_2 Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
shingle_title_3 Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
shingle_title_4 Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
timestamp 2025-06-30T23:31:48.376Z
titel Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
titel_suche Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax
topic W
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TE-TZ
SQ-SU
WW-YZ
TA-TD
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uid ipn_articles_6130867