Antimicrobial polypeptides of human vernix caseosa and amniotic fluid: Implications for newborn innate defense
Antimicrobial peptides/proteins are widespread in nature and play a critical role in host defense. To investigate whether these components contribute to surface protection of newborns at birth, we have characterized antimicrobial polypeptides in vernix caseosa (vernix) and amniotic fluid (AF). Conce...
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| Veröffentlicht in: | Pediatric research 2003-02, Vol.53 (2), p.211-216 |
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| creator | YOSHIO, Hiroyuki TOLLIN, Maria GUDMUNDSSON, Gudmundur H LAGERCRANTZ, Hugo JÖRNVALL, Hans MARCHINI, Giovanna AGERBERTH, Birgitta |
| description | Antimicrobial peptides/proteins are widespread in nature and play a critical role in host defense. To investigate whether these components contribute to surface protection of newborns at birth, we have characterized antimicrobial polypeptides in vernix caseosa (vernix) and amniotic fluid (AF). Concentrated peptide/protein extracts were obtained from 11 samples of vernix and six samples of AF and analyzed for antimicrobial activity using an inhibition zone assay. Proteins/peptides in all vernix extracts exhibited strong antibacterial activity against Bacillus megaterium (strain Bm11), in addition to antifungal activity against Candida albicans, whereas AF-derived proteins/peptides showed only the former activity. Fractions obtained after separation by reverse-phase HPLC exhibited antibacterial activity, with the most pronounced activity in a fraction containing alpha-defensins (HNP1-3). The presence of HNP1-3 was proved by dot blot analysis and confirmed by mass spectrometry. Lysozyme and ubiquitin were identified by sequence analysis in two fractions with antibacterial activity. Fractions of vernix and AF were also positive for LL-37 with dot blot and Western blot analyses, and one fraction apparently contained an extended form of LL-37. Interestingly, psoriasin, a calcium-binding protein that is up-regulated in psoriatic skin and was found recently to exhibit antimicrobial activity, was characterized in the vernix extract. The presence of all of these antimicrobial polypeptides in vernix suggests that they are important for surface defense and may have an active biologic role against microbial invasion at birth. |
| doi_str_mv | 10.1203/00006450-200302000-00003 |
| format | Article |
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To investigate whether these components contribute to surface protection of newborns at birth, we have characterized antimicrobial polypeptides in vernix caseosa (vernix) and amniotic fluid (AF). Concentrated peptide/protein extracts were obtained from 11 samples of vernix and six samples of AF and analyzed for antimicrobial activity using an inhibition zone assay. Proteins/peptides in all vernix extracts exhibited strong antibacterial activity against Bacillus megaterium (strain Bm11), in addition to antifungal activity against Candida albicans, whereas AF-derived proteins/peptides showed only the former activity. Fractions obtained after separation by reverse-phase HPLC exhibited antibacterial activity, with the most pronounced activity in a fraction containing alpha-defensins (HNP1-3). The presence of HNP1-3 was proved by dot blot analysis and confirmed by mass spectrometry. Lysozyme and ubiquitin were identified by sequence analysis in two fractions with antibacterial activity. Fractions of vernix and AF were also positive for LL-37 with dot blot and Western blot analyses, and one fraction apparently contained an extended form of LL-37. Interestingly, psoriasin, a calcium-binding protein that is up-regulated in psoriatic skin and was found recently to exhibit antimicrobial activity, was characterized in the vernix extract. The presence of all of these antimicrobial polypeptides in vernix suggests that they are important for surface defense and may have an active biologic role against microbial invasion at birth.</description><identifier>ISSN: 0031-3998</identifier><identifier>EISSN: 1530-0447</identifier><identifier>DOI: 10.1203/00006450-200302000-00003</identifier><identifier>PMID: 12538777</identifier><identifier>CODEN: PEREBL</identifier><language>eng</language><publisher>Hagerstown, MD: Lippincott Williams & Wilkins</publisher><subject>alpha-Defensins - analysis ; alpha-Defensins - physiology ; Amniotic Fluid - chemistry ; Amniotic Fluid - immunology ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - isolation & purification ; Antimicrobial Cationic Peptides - physiology ; Biological and medical sciences ; Calcium-Binding Proteins - analysis ; Calcium-Binding Proteins - physiology ; Chemotactic Factors - analysis ; Chemotactic Factors - physiology ; Delivery. Postpartum. Lactation ; Gynecology. Andrology. Obstetrics ; Humans ; Immunity, Innate ; Infant, Newborn ; Maternal, fetal and perinatal monitoring ; Medical sciences ; Muramidase - analysis ; Muramidase - physiology ; Peptides - chemistry ; Peptides - isolation & purification ; Peptides - metabolism ; S100 Calcium Binding Protein A7 ; S100 Proteins ; Ubiquitin - analysis ; Ubiquitin - physiology ; Vernix Caseosa - chemistry ; Vernix Caseosa - immunology</subject><ispartof>Pediatric research, 2003-02, Vol.53 (2), p.211-216</ispartof><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c322t-e7339bc3cd2113aabcb322e1f381ae5ee1b31f00e6db9823ebe97a4a2082b3d43</citedby><cites>FETCH-LOGICAL-c322t-e7339bc3cd2113aabcb322e1f381ae5ee1b31f00e6db9823ebe97a4a2082b3d43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14497648$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12538777$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>YOSHIO, Hiroyuki</creatorcontrib><creatorcontrib>TOLLIN, Maria</creatorcontrib><creatorcontrib>GUDMUNDSSON, Gudmundur H</creatorcontrib><creatorcontrib>LAGERCRANTZ, Hugo</creatorcontrib><creatorcontrib>JÖRNVALL, Hans</creatorcontrib><creatorcontrib>MARCHINI, Giovanna</creatorcontrib><creatorcontrib>AGERBERTH, Birgitta</creatorcontrib><title>Antimicrobial polypeptides of human vernix caseosa and amniotic fluid: Implications for newborn innate defense</title><title>Pediatric research</title><addtitle>Pediatr Res</addtitle><description>Antimicrobial peptides/proteins are widespread in nature and play a critical role in host defense. To investigate whether these components contribute to surface protection of newborns at birth, we have characterized antimicrobial polypeptides in vernix caseosa (vernix) and amniotic fluid (AF). Concentrated peptide/protein extracts were obtained from 11 samples of vernix and six samples of AF and analyzed for antimicrobial activity using an inhibition zone assay. Proteins/peptides in all vernix extracts exhibited strong antibacterial activity against Bacillus megaterium (strain Bm11), in addition to antifungal activity against Candida albicans, whereas AF-derived proteins/peptides showed only the former activity. Fractions obtained after separation by reverse-phase HPLC exhibited antibacterial activity, with the most pronounced activity in a fraction containing alpha-defensins (HNP1-3). The presence of HNP1-3 was proved by dot blot analysis and confirmed by mass spectrometry. Lysozyme and ubiquitin were identified by sequence analysis in two fractions with antibacterial activity. Fractions of vernix and AF were also positive for LL-37 with dot blot and Western blot analyses, and one fraction apparently contained an extended form of LL-37. Interestingly, psoriasin, a calcium-binding protein that is up-regulated in psoriatic skin and was found recently to exhibit antimicrobial activity, was characterized in the vernix extract. The presence of all of these antimicrobial polypeptides in vernix suggests that they are important for surface defense and may have an active biologic role against microbial invasion at birth.</description><subject>alpha-Defensins - analysis</subject><subject>alpha-Defensins - physiology</subject><subject>Amniotic Fluid - chemistry</subject><subject>Amniotic Fluid - immunology</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - isolation & purification</subject><subject>Antimicrobial Cationic Peptides - physiology</subject><subject>Biological and medical sciences</subject><subject>Calcium-Binding Proteins - analysis</subject><subject>Calcium-Binding Proteins - physiology</subject><subject>Chemotactic Factors - analysis</subject><subject>Chemotactic Factors - physiology</subject><subject>Delivery. Postpartum. Lactation</subject><subject>Gynecology. Andrology. Obstetrics</subject><subject>Humans</subject><subject>Immunity, Innate</subject><subject>Infant, Newborn</subject><subject>Maternal, fetal and perinatal monitoring</subject><subject>Medical sciences</subject><subject>Muramidase - analysis</subject><subject>Muramidase - physiology</subject><subject>Peptides - chemistry</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - metabolism</subject><subject>S100 Calcium Binding Protein A7</subject><subject>S100 Proteins</subject><subject>Ubiquitin - analysis</subject><subject>Ubiquitin - physiology</subject><subject>Vernix Caseosa - chemistry</subject><subject>Vernix Caseosa - immunology</subject><issn>0031-3998</issn><issn>1530-0447</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1vFSEUhonR2NvqXzBsdDcVOMyFcdc0fjRp4kbXkwNziJgZGGFG7b-X2qtlAeHN856TPIxxKS6lEvBWtHPUveiUECDaJbr7CJ6wg-yhfbQ2T9mhJbKDYbBn7LzW70JI3Vv9nJ1J1YM1xhxYukpbXKIv2UWc-Zrnu5XWLU5UeQ78275g4j-ppPibe6yUK3JME8clxbxFz8O8x-kdv1nWOXrcYk6Vh1x4ol8ul8RjSrgRnyhQqvSCPQs4V3p5ei_Y1w_vv1x_6m4_f7y5vrrtPCi1dWQABufBT0pKQHTetZxkACuReiLpQAYh6Di5wSogR4NBjUpY5WDScMHePMxdS_6xU93GJVZP84yJ8l5HowajpBUNtA9gM1BroTCuJS5Y7kYpxnvX4z_X43_XfyNo1VenHbtbaHosnuQ24PUJwOpxDgWTj_WR03owR23hD8pbiOI</recordid><startdate>20030201</startdate><enddate>20030201</enddate><creator>YOSHIO, Hiroyuki</creator><creator>TOLLIN, Maria</creator><creator>GUDMUNDSSON, Gudmundur H</creator><creator>LAGERCRANTZ, Hugo</creator><creator>JÖRNVALL, Hans</creator><creator>MARCHINI, Giovanna</creator><creator>AGERBERTH, Birgitta</creator><general>Lippincott Williams & Wilkins</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>20030201</creationdate><title>Antimicrobial polypeptides of human vernix caseosa and amniotic fluid: Implications for newborn innate defense</title><author>YOSHIO, Hiroyuki ; TOLLIN, Maria ; GUDMUNDSSON, Gudmundur H ; LAGERCRANTZ, Hugo ; JÖRNVALL, Hans ; MARCHINI, Giovanna ; AGERBERTH, Birgitta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c322t-e7339bc3cd2113aabcb322e1f381ae5ee1b31f00e6db9823ebe97a4a2082b3d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>alpha-Defensins - analysis</topic><topic>alpha-Defensins - physiology</topic><topic>Amniotic Fluid - chemistry</topic><topic>Amniotic Fluid - immunology</topic><topic>Anti-Bacterial Agents - chemistry</topic><topic>Anti-Bacterial Agents - isolation & purification</topic><topic>Antimicrobial Cationic Peptides - physiology</topic><topic>Biological and medical sciences</topic><topic>Calcium-Binding Proteins - analysis</topic><topic>Calcium-Binding Proteins - physiology</topic><topic>Chemotactic Factors - analysis</topic><topic>Chemotactic Factors - physiology</topic><topic>Delivery. Postpartum. Lactation</topic><topic>Gynecology. Andrology. Obstetrics</topic><topic>Humans</topic><topic>Immunity, Innate</topic><topic>Infant, Newborn</topic><topic>Maternal, fetal and perinatal monitoring</topic><topic>Medical sciences</topic><topic>Muramidase - analysis</topic><topic>Muramidase - physiology</topic><topic>Peptides - chemistry</topic><topic>Peptides - isolation & purification</topic><topic>Peptides - metabolism</topic><topic>S100 Calcium Binding Protein A7</topic><topic>S100 Proteins</topic><topic>Ubiquitin - analysis</topic><topic>Ubiquitin - physiology</topic><topic>Vernix Caseosa - chemistry</topic><topic>Vernix Caseosa - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>YOSHIO, Hiroyuki</creatorcontrib><creatorcontrib>TOLLIN, Maria</creatorcontrib><creatorcontrib>GUDMUNDSSON, Gudmundur H</creatorcontrib><creatorcontrib>LAGERCRANTZ, Hugo</creatorcontrib><creatorcontrib>JÖRNVALL, Hans</creatorcontrib><creatorcontrib>MARCHINI, Giovanna</creatorcontrib><creatorcontrib>AGERBERTH, Birgitta</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>Pediatric research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>YOSHIO, Hiroyuki</au><au>TOLLIN, Maria</au><au>GUDMUNDSSON, Gudmundur H</au><au>LAGERCRANTZ, Hugo</au><au>JÖRNVALL, Hans</au><au>MARCHINI, Giovanna</au><au>AGERBERTH, Birgitta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antimicrobial polypeptides of human vernix caseosa and amniotic fluid: Implications for newborn innate defense</atitle><jtitle>Pediatric research</jtitle><addtitle>Pediatr Res</addtitle><date>2003-02-01</date><risdate>2003</risdate><volume>53</volume><issue>2</issue><spage>211</spage><epage>216</epage><pages>211-216</pages><issn>0031-3998</issn><eissn>1530-0447</eissn><coden>PEREBL</coden><abstract>Antimicrobial peptides/proteins are widespread in nature and play a critical role in host defense. To investigate whether these components contribute to surface protection of newborns at birth, we have characterized antimicrobial polypeptides in vernix caseosa (vernix) and amniotic fluid (AF). Concentrated peptide/protein extracts were obtained from 11 samples of vernix and six samples of AF and analyzed for antimicrobial activity using an inhibition zone assay. Proteins/peptides in all vernix extracts exhibited strong antibacterial activity against Bacillus megaterium (strain Bm11), in addition to antifungal activity against Candida albicans, whereas AF-derived proteins/peptides showed only the former activity. Fractions obtained after separation by reverse-phase HPLC exhibited antibacterial activity, with the most pronounced activity in a fraction containing alpha-defensins (HNP1-3). The presence of HNP1-3 was proved by dot blot analysis and confirmed by mass spectrometry. Lysozyme and ubiquitin were identified by sequence analysis in two fractions with antibacterial activity. Fractions of vernix and AF were also positive for LL-37 with dot blot and Western blot analyses, and one fraction apparently contained an extended form of LL-37. Interestingly, psoriasin, a calcium-binding protein that is up-regulated in psoriatic skin and was found recently to exhibit antimicrobial activity, was characterized in the vernix extract. The presence of all of these antimicrobial polypeptides in vernix suggests that they are important for surface defense and may have an active biologic role against microbial invasion at birth.</abstract><cop>Hagerstown, MD</cop><pub>Lippincott Williams & Wilkins</pub><pmid>12538777</pmid><doi>10.1203/00006450-200302000-00003</doi><tpages>6</tpages></addata></record> |
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| ispartof | Pediatric research, 2003-02, Vol.53 (2), p.211-216 |
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| source | MEDLINE; SpringerLink Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection; Journals@Ovid Complete |
| subjects | alpha-Defensins - analysis alpha-Defensins - physiology Amniotic Fluid - chemistry Amniotic Fluid - immunology Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - isolation & purification Antimicrobial Cationic Peptides - physiology Biological and medical sciences Calcium-Binding Proteins - analysis Calcium-Binding Proteins - physiology Chemotactic Factors - analysis Chemotactic Factors - physiology Delivery. Postpartum. Lactation Gynecology. Andrology. Obstetrics Humans Immunity, Innate Infant, Newborn Maternal, fetal and perinatal monitoring Medical sciences Muramidase - analysis Muramidase - physiology Peptides - chemistry Peptides - isolation & purification Peptides - metabolism S100 Calcium Binding Protein A7 S100 Proteins Ubiquitin - analysis Ubiquitin - physiology Vernix Caseosa - chemistry Vernix Caseosa - immunology |
| title | Antimicrobial polypeptides of human vernix caseosa and amniotic fluid: Implications for newborn innate defense |
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