Host ICAMs play a role in cell invasion by Mycobacterium tuberculosis and Plasmodium falciparum
Intercellular adhesion molecules (ICAMs) belong to the immunoglobulin superfamily and participate in diverse cellular processes including host–pathogen interactions. ICAM-1 is expressed on various cell types including macrophages, whereas ICAM-4 is restricted to red blood cells. Here we report the i...
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| Veröffentlicht in: | Nature communications 2015-01, Vol.6 (1), p.6049-6049, Article 6049 |
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| creator | Bhalla, Kuhulika Chugh, Monika Mehrotra, Sonali Rathore, Sumit Tousif, Sultan Prakash Dwivedi, Ved Prakash, Prem Kumar Samuchiwal, Sachin Kumar, Sushil Kumar Singh, Dhiraj Ghanwat, Swapnil Kumar, Dhiraj Das, Gobardhan Mohmmed, Asif Malhotra, Pawan Ranganathan, Anand |
| description | Intercellular adhesion molecules (ICAMs) belong to the immunoglobulin superfamily and participate in diverse cellular processes including host–pathogen interactions. ICAM-1 is expressed on various cell types including macrophages, whereas ICAM-4 is restricted to red blood cells. Here we report the identification of an 11-kDa synthetic protein, M5, that binds to human ICAM-1 and ICAM-4, as shown by
in vitro
interaction studies, surface plasmon resonance and immunolocalization. M5 greatly inhibits the invasion of macrophages and erythrocytes by
Mycobacterium tuberculosis
and
Plasmodium falciparum
, respectively. Pharmacological and siRNA-mediated inhibition of ICAM-1 expression also results in reduced
M. tuberculosis
invasion of macrophages. ICAM-4 binds to
P. falciparum
merozoites, and the addition of recombinant ICAM-4 to parasite cultures blocks invasion of erythrocytes by newly released merozoites. Our results indicate that ICAM-1 and ICAM-4 play roles in host cell invasion by
M. tuberculosis
and
P. falciparum
, respectively, either as receptors or as crucial accessory molecules.
Intercellular adhesion molecules (ICAMs) participate in cellular processes such as host-pathogen interactions. Here, the authors show that ICAM-1 and ICAM-4 play roles in the invasion of macrophages and red blood cells by
Mycobacterium tuberculosis
and
Plasmodium falciparum
, respectively. |
| doi_str_mv | 10.1038/ncomms7049 |
| format | Article |
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in vitro
interaction studies, surface plasmon resonance and immunolocalization. M5 greatly inhibits the invasion of macrophages and erythrocytes by
Mycobacterium tuberculosis
and
Plasmodium falciparum
, respectively. Pharmacological and siRNA-mediated inhibition of ICAM-1 expression also results in reduced
M. tuberculosis
invasion of macrophages. ICAM-4 binds to
P. falciparum
merozoites, and the addition of recombinant ICAM-4 to parasite cultures blocks invasion of erythrocytes by newly released merozoites. Our results indicate that ICAM-1 and ICAM-4 play roles in host cell invasion by
M. tuberculosis
and
P. falciparum
, respectively, either as receptors or as crucial accessory molecules.
Intercellular adhesion molecules (ICAMs) participate in cellular processes such as host-pathogen interactions. Here, the authors show that ICAM-1 and ICAM-4 play roles in the invasion of macrophages and red blood cells by
Mycobacterium tuberculosis
and
Plasmodium falciparum
, respectively.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/ncomms7049</identifier><identifier>PMID: 25586702</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13/106 ; 13/109 ; 13/31 ; 13/51 ; 14/19 ; 631/326/41/2531 ; 631/80/79 ; 631/80/84/2336 ; 82/103 ; 82/80 ; Animals ; Antigens ; Biotechnology ; Cell Adhesion Molecules - metabolism ; Cell Line ; Drug resistance ; Erythrocytes - parasitology ; Female ; Genetic engineering ; Host-Pathogen Interactions ; Humanities and Social Sciences ; Humans ; Infections ; Intercellular Adhesion Molecule-1 - chemistry ; Intercellular Adhesion Molecule-1 - metabolism ; Malaria ; Malaria, Falciparum - parasitology ; Merozoites - physiology ; Mice, Inbred BALB C ; multidisciplinary ; Mycobacterium tuberculosis - genetics ; Mycobacterium tuberculosis - physiology ; Parasites ; Pathogens ; Plasmodium falciparum - physiology ; Protein Binding ; Protein Interaction Mapping ; Protein Multimerization ; Protein Structure, Tertiary ; Proteins ; Science ; Science (multidisciplinary) ; Tuberculosis ; Tuberculosis - microbiology ; Two-Hybrid System Techniques ; West Nile virus</subject><ispartof>Nature communications, 2015-01, Vol.6 (1), p.6049-6049, Article 6049</ispartof><rights>Springer Nature Limited 2015</rights><rights>Copyright Nature Publishing Group Jan 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c453t-4cbaa5b2119a0744eb7e895ed04e215e5d9228f8a71e5df8f3bfea13e29c58df3</citedby><cites>FETCH-LOGICAL-c453t-4cbaa5b2119a0744eb7e895ed04e215e5d9228f8a71e5df8f3bfea13e29c58df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ncomms7049$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://doi.org/10.1038/ncomms7049$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,864,27924,27925,41120,42189,51576</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/ncomms7049$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25586702$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bhalla, Kuhulika</creatorcontrib><creatorcontrib>Chugh, Monika</creatorcontrib><creatorcontrib>Mehrotra, Sonali</creatorcontrib><creatorcontrib>Rathore, Sumit</creatorcontrib><creatorcontrib>Tousif, Sultan</creatorcontrib><creatorcontrib>Prakash Dwivedi, Ved</creatorcontrib><creatorcontrib>Prakash, Prem</creatorcontrib><creatorcontrib>Kumar Samuchiwal, Sachin</creatorcontrib><creatorcontrib>Kumar, Sushil</creatorcontrib><creatorcontrib>Kumar Singh, Dhiraj</creatorcontrib><creatorcontrib>Ghanwat, Swapnil</creatorcontrib><creatorcontrib>Kumar, Dhiraj</creatorcontrib><creatorcontrib>Das, Gobardhan</creatorcontrib><creatorcontrib>Mohmmed, Asif</creatorcontrib><creatorcontrib>Malhotra, Pawan</creatorcontrib><creatorcontrib>Ranganathan, Anand</creatorcontrib><title>Host ICAMs play a role in cell invasion by Mycobacterium tuberculosis and Plasmodium falciparum</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><addtitle>Nat Commun</addtitle><description>Intercellular adhesion molecules (ICAMs) belong to the immunoglobulin superfamily and participate in diverse cellular processes including host–pathogen interactions. ICAM-1 is expressed on various cell types including macrophages, whereas ICAM-4 is restricted to red blood cells. Here we report the identification of an 11-kDa synthetic protein, M5, that binds to human ICAM-1 and ICAM-4, as shown by
in vitro
interaction studies, surface plasmon resonance and immunolocalization. M5 greatly inhibits the invasion of macrophages and erythrocytes by
Mycobacterium tuberculosis
and
Plasmodium falciparum
, respectively. Pharmacological and siRNA-mediated inhibition of ICAM-1 expression also results in reduced
M. tuberculosis
invasion of macrophages. ICAM-4 binds to
P. falciparum
merozoites, and the addition of recombinant ICAM-4 to parasite cultures blocks invasion of erythrocytes by newly released merozoites. Our results indicate that ICAM-1 and ICAM-4 play roles in host cell invasion by
M. tuberculosis
and
P. falciparum
, respectively, either as receptors or as crucial accessory molecules.
Intercellular adhesion molecules (ICAMs) participate in cellular processes such as host-pathogen interactions. Here, the authors show that ICAM-1 and ICAM-4 play roles in the invasion of macrophages and red blood cells by
Mycobacterium tuberculosis
and
Plasmodium falciparum
, respectively.</description><subject>13/106</subject><subject>13/109</subject><subject>13/31</subject><subject>13/51</subject><subject>14/19</subject><subject>631/326/41/2531</subject><subject>631/80/79</subject><subject>631/80/84/2336</subject><subject>82/103</subject><subject>82/80</subject><subject>Animals</subject><subject>Antigens</subject><subject>Biotechnology</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Line</subject><subject>Drug resistance</subject><subject>Erythrocytes - parasitology</subject><subject>Female</subject><subject>Genetic engineering</subject><subject>Host-Pathogen Interactions</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Infections</subject><subject>Intercellular Adhesion Molecule-1 - chemistry</subject><subject>Intercellular Adhesion Molecule-1 - metabolism</subject><subject>Malaria</subject><subject>Malaria, Falciparum - parasitology</subject><subject>Merozoites - physiology</subject><subject>Mice, Inbred BALB C</subject><subject>multidisciplinary</subject><subject>Mycobacterium tuberculosis - genetics</subject><subject>Mycobacterium tuberculosis - physiology</subject><subject>Parasites</subject><subject>Pathogens</subject><subject>Plasmodium falciparum - physiology</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Tuberculosis</subject><subject>Tuberculosis - microbiology</subject><subject>Two-Hybrid System Techniques</subject><subject>West Nile virus</subject><issn>2041-1723</issn><issn>2041-1723</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNplkE1Lw0AQhhdRrNRe_AGy4EWU6n42m6MUtUKLHvQcNpuJpGSzcTcR8u_d0qpF5zIzzMM7My9CZ5TcUMLVbWOctSEhIj1AJ4wIOqUJ44d79QhNQliTGDylSohjNGJSqllC2AnKFi50-Gl-twq4rfWANfauBlw12EBdx_ypQ-UanA94NRiXa9OBr3qLuz4Hb_rahSpg3RT4pdbBumIzK3Vtqlb73p6io9gEmOzyGL093L_OF9Pl82PcupwaIXk3FSbXWuaM0lSTRAjIE1CphIIIYFSCLFLGVKl0QmNdqpLnJWjKgaVGqqLkY3S51W29--ghdJmtwuYD3YDrQ0ZnkglCpWQRvfiDrl3vm3hdpIRklCdSRupqSxnvQvBQZq2vrPZDRkm2cT77dT7C5zvJPrdQ_KDfPkfgeguEOGrewe_t_C_3BZ4ljk0</recordid><startdate>20150114</startdate><enddate>20150114</enddate><creator>Bhalla, Kuhulika</creator><creator>Chugh, Monika</creator><creator>Mehrotra, Sonali</creator><creator>Rathore, Sumit</creator><creator>Tousif, Sultan</creator><creator>Prakash Dwivedi, Ved</creator><creator>Prakash, Prem</creator><creator>Kumar Samuchiwal, Sachin</creator><creator>Kumar, Sushil</creator><creator>Kumar Singh, Dhiraj</creator><creator>Ghanwat, Swapnil</creator><creator>Kumar, Dhiraj</creator><creator>Das, Gobardhan</creator><creator>Mohmmed, Asif</creator><creator>Malhotra, Pawan</creator><creator>Ranganathan, Anand</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7TO</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>20150114</creationdate><title>Host ICAMs play a role in cell invasion by Mycobacterium tuberculosis and Plasmodium falciparum</title><author>Bhalla, Kuhulika ; Chugh, Monika ; Mehrotra, Sonali ; Rathore, Sumit ; Tousif, Sultan ; Prakash Dwivedi, Ved ; Prakash, Prem ; Kumar Samuchiwal, Sachin ; Kumar, Sushil ; Kumar Singh, Dhiraj ; Ghanwat, Swapnil ; Kumar, Dhiraj ; Das, Gobardhan ; Mohmmed, Asif ; Malhotra, Pawan ; Ranganathan, Anand</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c453t-4cbaa5b2119a0744eb7e895ed04e215e5d9228f8a71e5df8f3bfea13e29c58df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>13/106</topic><topic>13/109</topic><topic>13/31</topic><topic>13/51</topic><topic>14/19</topic><topic>631/326/41/2531</topic><topic>631/80/79</topic><topic>631/80/84/2336</topic><topic>82/103</topic><topic>82/80</topic><topic>Animals</topic><topic>Antigens</topic><topic>Biotechnology</topic><topic>Cell Adhesion Molecules - 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Academic</collection><jtitle>Nature communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Bhalla, Kuhulika</au><au>Chugh, Monika</au><au>Mehrotra, Sonali</au><au>Rathore, Sumit</au><au>Tousif, Sultan</au><au>Prakash Dwivedi, Ved</au><au>Prakash, Prem</au><au>Kumar Samuchiwal, Sachin</au><au>Kumar, Sushil</au><au>Kumar Singh, Dhiraj</au><au>Ghanwat, Swapnil</au><au>Kumar, Dhiraj</au><au>Das, Gobardhan</au><au>Mohmmed, Asif</au><au>Malhotra, Pawan</au><au>Ranganathan, Anand</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Host ICAMs play a role in cell invasion by Mycobacterium tuberculosis and Plasmodium falciparum</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2015-01-14</date><risdate>2015</risdate><volume>6</volume><issue>1</issue><spage>6049</spage><epage>6049</epage><pages>6049-6049</pages><artnum>6049</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>Intercellular adhesion molecules (ICAMs) belong to the immunoglobulin superfamily and participate in diverse cellular processes including host–pathogen interactions. ICAM-1 is expressed on various cell types including macrophages, whereas ICAM-4 is restricted to red blood cells. Here we report the identification of an 11-kDa synthetic protein, M5, that binds to human ICAM-1 and ICAM-4, as shown by
in vitro
interaction studies, surface plasmon resonance and immunolocalization. M5 greatly inhibits the invasion of macrophages and erythrocytes by
Mycobacterium tuberculosis
and
Plasmodium falciparum
, respectively. Pharmacological and siRNA-mediated inhibition of ICAM-1 expression also results in reduced
M. tuberculosis
invasion of macrophages. ICAM-4 binds to
P. falciparum
merozoites, and the addition of recombinant ICAM-4 to parasite cultures blocks invasion of erythrocytes by newly released merozoites. Our results indicate that ICAM-1 and ICAM-4 play roles in host cell invasion by
M. tuberculosis
and
P. falciparum
, respectively, either as receptors or as crucial accessory molecules.
Intercellular adhesion molecules (ICAMs) participate in cellular processes such as host-pathogen interactions. Here, the authors show that ICAM-1 and ICAM-4 play roles in the invasion of macrophages and red blood cells by
Mycobacterium tuberculosis
and
Plasmodium falciparum
, respectively.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>25586702</pmid><doi>10.1038/ncomms7049</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Nature communications, 2015-01, Vol.6 (1), p.6049-6049, Article 6049 |
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| subjects | 13/106 13/109 13/31 13/51 14/19 631/326/41/2531 631/80/79 631/80/84/2336 82/103 82/80 Animals Antigens Biotechnology Cell Adhesion Molecules - metabolism Cell Line Drug resistance Erythrocytes - parasitology Female Genetic engineering Host-Pathogen Interactions Humanities and Social Sciences Humans Infections Intercellular Adhesion Molecule-1 - chemistry Intercellular Adhesion Molecule-1 - metabolism Malaria Malaria, Falciparum - parasitology Merozoites - physiology Mice, Inbred BALB C multidisciplinary Mycobacterium tuberculosis - genetics Mycobacterium tuberculosis - physiology Parasites Pathogens Plasmodium falciparum - physiology Protein Binding Protein Interaction Mapping Protein Multimerization Protein Structure, Tertiary Proteins Science Science (multidisciplinary) Tuberculosis Tuberculosis - microbiology Two-Hybrid System Techniques West Nile virus |
| title | Host ICAMs play a role in cell invasion by Mycobacterium tuberculosis and Plasmodium falciparum |
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