Complement factor H in host defense and immune evasion
Complement is the major humoral component of the innate immune system. It recognizes pathogen - and damage - associated molecular patterns , and initiates the immune response in coordination with innate and adaptive immunity. When activated, the complement system unleashes powerful cytotoxic and inf...
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creator | Parente, Raffaella Clark, Simon J. Inforzato, Antonio Day, Anthony J. |
description | Complement is the major humoral component of the innate immune system. It recognizes
pathogen
- and
damage
-
associated molecular patterns
, and initiates the immune response in coordination with innate and adaptive immunity. When activated, the complement system unleashes powerful cytotoxic and inflammatory mechanisms, and thus its tight control is crucial to prevent damage to host tissues and allow restoration of immune homeostasis. Factor H is the major soluble inhibitor of complement, where its binding to
self markers
(i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of
self
by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e.,
non
-
self
) and cancer cells (i.e.,
altered
-
self
) can hijack factor H to evade the immune response. Here we review recent (and not so recent) literature on the structure and function of factor H, including the emerging roles of this protein in the pathophysiology of infectious diseases and cancer. |
doi_str_mv | 10.1007/s00018-016-2418-4 |
format | Article |
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pathogen
- and
damage
-
associated molecular patterns
, and initiates the immune response in coordination with innate and adaptive immunity. When activated, the complement system unleashes powerful cytotoxic and inflammatory mechanisms, and thus its tight control is crucial to prevent damage to host tissues and allow restoration of immune homeostasis. Factor H is the major soluble inhibitor of complement, where its binding to
self markers
(i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of
self
by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e.,
non
-
self
) and cancer cells (i.e.,
altered
-
self
) can hijack factor H to evade the immune response. Here we review recent (and not so recent) literature on the structure and function of factor H, including the emerging roles of this protein in the pathophysiology of infectious diseases and cancer.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-016-2418-4</identifier><identifier>PMID: 27942748</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>adaptive immunity ; Animals ; Biochemistry ; Biomarkers ; Biomedical and Life Sciences ; Biomedicine ; Cancer ; Cell Biology ; complement ; Complement Factor H - chemistry ; Complement Factor H - metabolism ; cytotoxicity ; Disease ; homeostasis ; Humans ; Immune Evasion ; Immune response ; Immune system ; Immunity, Innate ; Infectious diseases ; Inflammatory diseases ; innate immunity ; Life Sciences ; Macular degeneration ; mutation ; neoplasm cells ; neoplasms ; Pathogens ; pathophysiology ; Polysaccharides - metabolism ; Protein Binding ; Review</subject><ispartof>Cellular and molecular life sciences : CMLS, 2017-05, Vol.74 (9), p.1605-1624</ispartof><rights>The Author(s) 2016</rights><rights>Cellular and Molecular Life Sciences is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c602t-6a5873a530ea0edd1a7c8a19962e37caeea3d9cfbf83664866c5c278c8a590d13</citedby><cites>FETCH-LOGICAL-c602t-6a5873a530ea0edd1a7c8a19962e37caeea3d9cfbf83664866c5c278c8a590d13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5378756/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5378756/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,41467,42536,51298,53770,53772</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27942748$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Parente, Raffaella</creatorcontrib><creatorcontrib>Clark, Simon J.</creatorcontrib><creatorcontrib>Inforzato, Antonio</creatorcontrib><creatorcontrib>Day, Anthony J.</creatorcontrib><title>Complement factor H in host defense and immune evasion</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell. Mol. Life Sci</addtitle><addtitle>Cell Mol Life Sci</addtitle><description>Complement is the major humoral component of the innate immune system. It recognizes
pathogen
- and
damage
-
associated molecular patterns
, and initiates the immune response in coordination with innate and adaptive immunity. When activated, the complement system unleashes powerful cytotoxic and inflammatory mechanisms, and thus its tight control is crucial to prevent damage to host tissues and allow restoration of immune homeostasis. Factor H is the major soluble inhibitor of complement, where its binding to
self markers
(i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of
self
by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e.,
non
-
self
) and cancer cells (i.e.,
altered
-
self
) can hijack factor H to evade the immune response. Here we review recent (and not so recent) literature on the structure and function of factor H, including the emerging roles of this protein in the pathophysiology of infectious diseases and cancer.</description><subject>adaptive immunity</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomarkers</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer</subject><subject>Cell Biology</subject><subject>complement</subject><subject>Complement Factor H - chemistry</subject><subject>Complement Factor H - metabolism</subject><subject>cytotoxicity</subject><subject>Disease</subject><subject>homeostasis</subject><subject>Humans</subject><subject>Immune Evasion</subject><subject>Immune response</subject><subject>Immune system</subject><subject>Immunity, Innate</subject><subject>Infectious diseases</subject><subject>Inflammatory diseases</subject><subject>innate immunity</subject><subject>Life Sciences</subject><subject>Macular degeneration</subject><subject>mutation</subject><subject>neoplasm cells</subject><subject>neoplasms</subject><subject>Pathogens</subject><subject>pathophysiology</subject><subject>Polysaccharides - metabolism</subject><subject>Protein Binding</subject><subject>Review</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkUtLxDAUhYMovn-AGym4cVPNO-lGkMEXCG4U3IWY3mqlTcakFfz3ZphxGAXR1b1wv3tucg5CBwSfEIzVacIYE11iIkvKc8PX0DbhFJcVVmR90UtNH7fQTkqvGRaayk20RVXFqeJ6G8lJ6Kcd9OCHorFuCLG4LlpfvIQ0FDU04BMU1tdF2_ejhwLebWqD30Mbje0S7C_qLnq4vLifXJe3d1c3k_Pb0klMh1JaoRWzgmGwGOqaWOW0JVUlKTDlLIBldeWap0YzKbmW0glHlc6QqHBN2C46m-tOx6ceapefGW1nprHtbfwwwbbm-8S3L-Y5vBvBlFZCZoHjhUAMbyOkwfRtctB11kMYk6HZQl5xpumfKNEV0Upxwv6BCipldllk9OgH-hrG6LNpmdKMK0zojCJzysWQUoRm-UWCzSxrM8_a5KzNLGvD887hqjfLja9wM0DnQMoj_wxx5fSvqp_kX7LN</recordid><startdate>20170501</startdate><enddate>20170501</enddate><creator>Parente, Raffaella</creator><creator>Clark, Simon J.</creator><creator>Inforzato, Antonio</creator><creator>Day, Anthony J.</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>C6C</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</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>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20170501</creationdate><title>Complement factor H in host defense and immune evasion</title><author>Parente, Raffaella ; Clark, Simon J. ; Inforzato, Antonio ; Day, Anthony J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c602t-6a5873a530ea0edd1a7c8a19962e37caeea3d9cfbf83664866c5c278c8a590d13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>adaptive immunity</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biomarkers</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cancer</topic><topic>Cell Biology</topic><topic>complement</topic><topic>Complement Factor H - chemistry</topic><topic>Complement Factor H - metabolism</topic><topic>cytotoxicity</topic><topic>Disease</topic><topic>homeostasis</topic><topic>Humans</topic><topic>Immune Evasion</topic><topic>Immune response</topic><topic>Immune system</topic><topic>Immunity, Innate</topic><topic>Infectious diseases</topic><topic>Inflammatory diseases</topic><topic>innate immunity</topic><topic>Life Sciences</topic><topic>Macular degeneration</topic><topic>mutation</topic><topic>neoplasm cells</topic><topic>neoplasms</topic><topic>Pathogens</topic><topic>pathophysiology</topic><topic>Polysaccharides - metabolism</topic><topic>Protein Binding</topic><topic>Review</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Parente, Raffaella</creatorcontrib><creatorcontrib>Clark, Simon J.</creatorcontrib><creatorcontrib>Inforzato, Antonio</creatorcontrib><creatorcontrib>Day, Anthony J.</creatorcontrib><collection>SpringerOpen</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cellular and molecular life sciences : CMLS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Parente, Raffaella</au><au>Clark, Simon J.</au><au>Inforzato, Antonio</au><au>Day, Anthony J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complement factor H in host defense and immune evasion</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><stitle>Cell. Mol. Life Sci</stitle><addtitle>Cell Mol Life Sci</addtitle><date>2017-05-01</date><risdate>2017</risdate><volume>74</volume><issue>9</issue><spage>1605</spage><epage>1624</epage><pages>1605-1624</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>Complement is the major humoral component of the innate immune system. It recognizes
pathogen
- and
damage
-
associated molecular patterns
, and initiates the immune response in coordination with innate and adaptive immunity. When activated, the complement system unleashes powerful cytotoxic and inflammatory mechanisms, and thus its tight control is crucial to prevent damage to host tissues and allow restoration of immune homeostasis. Factor H is the major soluble inhibitor of complement, where its binding to
self markers
(i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of
self
by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e.,
non
-
self
) and cancer cells (i.e.,
altered
-
self
) can hijack factor H to evade the immune response. Here we review recent (and not so recent) literature on the structure and function of factor H, including the emerging roles of this protein in the pathophysiology of infectious diseases and cancer.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>27942748</pmid><doi>10.1007/s00018-016-2418-4</doi><tpages>20</tpages><oa>free_for_read</oa></addata></record> |
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subjects | adaptive immunity Animals Biochemistry Biomarkers Biomedical and Life Sciences Biomedicine Cancer Cell Biology complement Complement Factor H - chemistry Complement Factor H - metabolism cytotoxicity Disease homeostasis Humans Immune Evasion Immune response Immune system Immunity, Innate Infectious diseases Inflammatory diseases innate immunity Life Sciences Macular degeneration mutation neoplasm cells neoplasms Pathogens pathophysiology Polysaccharides - metabolism Protein Binding Review |
title | Complement factor H in host defense and immune evasion |
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