Differential extraction and enrichment of human sperm surface proteins in a proteome: Identification of immunocontraceptive candidates
The objective of this study was to discover previously unknown human sperm surface proteins that may be candidate contraceptive vaccinogens. To this end, methods of concentrating human sperm proteins for microsequencing by mass spectrometry were used, which increased the likelihood of identifying su...
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| Veröffentlicht in: | Electrophoresis 2001-08, Vol.22 (14), p.3053-3066 |
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| creator | Shetty, Jagathpala Diekman, Alan B. Jayes, Friederike C. L. Sherman, Nicholas E. Naaby-Hansen, Soren Flickinger, Charles J. Herr, John C. |
| description | The objective of this study was to discover previously unknown human sperm surface proteins that may be candidate contraceptive vaccinogens. To this end, methods of concentrating human sperm proteins for microsequencing by mass spectrometry were used, which increased the likelihood of identifying surface proteins. Vectorial labeling, differential extraction and two‐dimensional (2‐D) gel electrophoresis were employed to identify and isolate proteins accessible at the cell surface. Percoll harvested or swim‐up sperm were either solubilized directly or solubilized after surface labeling with sulfo‐succinimidyl‐6‐(biotinamido)hexanoate (sulfo‐NHS‐LC‐biotin). Comparisons were made of proteins extracted with four lysis buffers: (i) Celis buffer containing 9.8 M urea and 2% Igepal CA‐630; (ii) 1% Triton X (TX)‐100; (iii) 1.7% TX‐114 followed by phase partitioning; or (iv) 1 M NaCl. Blots of proteins separated by high‐resolution 2‐D electrophoresis were probed with avidin and antibodies to known proteins specific for three domains: the sperm surface (SAGA‐1), the acrosome (SP‐10), and the cytoskeleton (α‐tubulin). Celis buffer (45 min) extracted proteins from all three major compartments. However, a 20‐s extraction in Celis buffer enriched for several proteins and enabled the identification of several novel peptides by mass spectrometry. Mild extraction with TX‐100 or 1 M NaCl solubilized mainly membrane and acrosomal proteins, but not cytoskeletal proteins. Comparison of biotinylated proteins extracted by each method showed that the major vectorially labeled proteins solubilized by Celis buffer were also solubilized by TX‐100, TX‐114, and 1 M NaCl. Extraction with TX‐114 followed by phase‐partitioning significantly enriched hydrophobic surface proteins and aided resolution and isolation. Eight protein spots microsequenced following all these extraction methods proved to be novel sperm molecules. |
| doi_str_mv | 10.1002/1522-2683(200108)22:14<3053::AID-ELPS3053>3.0.CO;2-K |
| format | Article |
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L. ; Sherman, Nicholas E. ; Naaby-Hansen, Soren ; Flickinger, Charles J. ; Herr, John C.</creator><creatorcontrib>Shetty, Jagathpala ; Diekman, Alan B. ; Jayes, Friederike C. L. ; Sherman, Nicholas E. ; Naaby-Hansen, Soren ; Flickinger, Charles J. ; Herr, John C.</creatorcontrib><description>The objective of this study was to discover previously unknown human sperm surface proteins that may be candidate contraceptive vaccinogens. To this end, methods of concentrating human sperm proteins for microsequencing by mass spectrometry were used, which increased the likelihood of identifying surface proteins. Vectorial labeling, differential extraction and two‐dimensional (2‐D) gel electrophoresis were employed to identify and isolate proteins accessible at the cell surface. Percoll harvested or swim‐up sperm were either solubilized directly or solubilized after surface labeling with sulfo‐succinimidyl‐6‐(biotinamido)hexanoate (sulfo‐NHS‐LC‐biotin). Comparisons were made of proteins extracted with four lysis buffers: (i) Celis buffer containing 9.8 M urea and 2% Igepal CA‐630; (ii) 1% Triton X (TX)‐100; (iii) 1.7% TX‐114 followed by phase partitioning; or (iv) 1 M NaCl. Blots of proteins separated by high‐resolution 2‐D electrophoresis were probed with avidin and antibodies to known proteins specific for three domains: the sperm surface (SAGA‐1), the acrosome (SP‐10), and the cytoskeleton (α‐tubulin). Celis buffer (45 min) extracted proteins from all three major compartments. However, a 20‐s extraction in Celis buffer enriched for several proteins and enabled the identification of several novel peptides by mass spectrometry. Mild extraction with TX‐100 or 1 M NaCl solubilized mainly membrane and acrosomal proteins, but not cytoskeletal proteins. Comparison of biotinylated proteins extracted by each method showed that the major vectorially labeled proteins solubilized by Celis buffer were also solubilized by TX‐100, TX‐114, and 1 M NaCl. Extraction with TX‐114 followed by phase‐partitioning significantly enriched hydrophobic surface proteins and aided resolution and isolation. Eight protein spots microsequenced following all these extraction methods proved to be novel sperm molecules.</description><identifier>ISSN: 0173-0835</identifier><identifier>EISSN: 1522-2683</identifier><identifier>DOI: 10.1002/1522-2683(200108)22:14<3053::AID-ELPS3053>3.0.CO;2-K</identifier><identifier>PMID: 11565800</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Acrosome - chemistry ; Adult ; Amino Acid Sequence ; Autoantibodies - blood ; Autoantibodies - immunology ; Autoantigens - analysis ; Autoantigens - isolation & purification ; Biotin - analogs & derivatives ; Biotinylation ; Blotting, Western ; Buffers ; Chemical Fractionation - methods ; Contraception, Immunologic ; Cytoskeletal Proteins - analysis ; Cytoskeletal Proteins - isolation & purification ; Detergents ; Differential extraction ; Electrophoresis, Gel, Two-Dimensional ; Human sperm ; Humans ; Immunocontraception ; Infertility, Male - blood ; Infertility, Male - immunology ; Isoelectric Focusing ; Male ; Membrane Proteins - analysis ; Membrane Proteins - isolation & purification ; Molecular Sequence Data ; Octoxynol ; Polyethylene Glycols ; Proteins - analysis ; Proteins - isolation & purification ; Proteome ; Saline Solution, Hypertonic ; Sequence Analysis, Protein ; Solubility ; Solvents ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Spermatozoa - chemistry ; Subtraction Technique ; Succinimides ; Two-dimensional gel electrophoresis ; Urea</subject><ispartof>Electrophoresis, 2001-08, Vol.22 (14), p.3053-3066</ispartof><rights>Copyright © 2001 WILEY‐VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4043-b6265327a0894adb541cd29b07e84bc877b342df9b9c1b01205f122b2d95ea533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F1522-2683%28200108%2922%3A14%3C3053%3A%3AAID-ELPS3053%3E3.0.CO%3B2-K$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F1522-2683%28200108%2922%3A14%3C3053%3A%3AAID-ELPS3053%3E3.0.CO%3B2-K$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11565800$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shetty, Jagathpala</creatorcontrib><creatorcontrib>Diekman, Alan B.</creatorcontrib><creatorcontrib>Jayes, Friederike C. L.</creatorcontrib><creatorcontrib>Sherman, Nicholas E.</creatorcontrib><creatorcontrib>Naaby-Hansen, Soren</creatorcontrib><creatorcontrib>Flickinger, Charles J.</creatorcontrib><creatorcontrib>Herr, John C.</creatorcontrib><title>Differential extraction and enrichment of human sperm surface proteins in a proteome: Identification of immunocontraceptive candidates</title><title>Electrophoresis</title><addtitle>ELECTROPHORESIS</addtitle><description>The objective of this study was to discover previously unknown human sperm surface proteins that may be candidate contraceptive vaccinogens. To this end, methods of concentrating human sperm proteins for microsequencing by mass spectrometry were used, which increased the likelihood of identifying surface proteins. Vectorial labeling, differential extraction and two‐dimensional (2‐D) gel electrophoresis were employed to identify and isolate proteins accessible at the cell surface. Percoll harvested or swim‐up sperm were either solubilized directly or solubilized after surface labeling with sulfo‐succinimidyl‐6‐(biotinamido)hexanoate (sulfo‐NHS‐LC‐biotin). Comparisons were made of proteins extracted with four lysis buffers: (i) Celis buffer containing 9.8 M urea and 2% Igepal CA‐630; (ii) 1% Triton X (TX)‐100; (iii) 1.7% TX‐114 followed by phase partitioning; or (iv) 1 M NaCl. Blots of proteins separated by high‐resolution 2‐D electrophoresis were probed with avidin and antibodies to known proteins specific for three domains: the sperm surface (SAGA‐1), the acrosome (SP‐10), and the cytoskeleton (α‐tubulin). Celis buffer (45 min) extracted proteins from all three major compartments. However, a 20‐s extraction in Celis buffer enriched for several proteins and enabled the identification of several novel peptides by mass spectrometry. Mild extraction with TX‐100 or 1 M NaCl solubilized mainly membrane and acrosomal proteins, but not cytoskeletal proteins. Comparison of biotinylated proteins extracted by each method showed that the major vectorially labeled proteins solubilized by Celis buffer were also solubilized by TX‐100, TX‐114, and 1 M NaCl. Extraction with TX‐114 followed by phase‐partitioning significantly enriched hydrophobic surface proteins and aided resolution and isolation. Eight protein spots microsequenced following all these extraction methods proved to be novel sperm molecules.</description><subject>Acrosome - chemistry</subject><subject>Adult</subject><subject>Amino Acid Sequence</subject><subject>Autoantibodies - blood</subject><subject>Autoantibodies - immunology</subject><subject>Autoantigens - analysis</subject><subject>Autoantigens - isolation & purification</subject><subject>Biotin - analogs & derivatives</subject><subject>Biotinylation</subject><subject>Blotting, Western</subject><subject>Buffers</subject><subject>Chemical Fractionation - methods</subject><subject>Contraception, Immunologic</subject><subject>Cytoskeletal Proteins - analysis</subject><subject>Cytoskeletal Proteins - isolation & purification</subject><subject>Detergents</subject><subject>Differential extraction</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Human sperm</subject><subject>Humans</subject><subject>Immunocontraception</subject><subject>Infertility, Male - blood</subject><subject>Infertility, Male - immunology</subject><subject>Isoelectric Focusing</subject><subject>Male</subject><subject>Membrane Proteins - analysis</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Molecular Sequence Data</subject><subject>Octoxynol</subject><subject>Polyethylene Glycols</subject><subject>Proteins - analysis</subject><subject>Proteins - isolation & purification</subject><subject>Proteome</subject><subject>Saline Solution, Hypertonic</subject><subject>Sequence Analysis, Protein</subject><subject>Solubility</subject><subject>Solvents</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Spermatozoa - chemistry</subject><subject>Subtraction Technique</subject><subject>Succinimides</subject><subject>Two-dimensional gel electrophoresis</subject><subject>Urea</subject><issn>0173-0835</issn><issn>1522-2683</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkUtv1DAUhSMEotPCX0BeIVhkuH5NkqFCamdKGTpiKlGemyvHcVRDHoOdQPsH-N04ZBhWLFhZxz73O9Y9UXRMYUoB2DMqGYvZLOVPGACF9CljcyqOOUg-n5-slvHZ-vLtoF7wKUwXm-csvrgTTfZjd6MJ0ITHkHJ5EB16_wUARCbE_eiAUjmTKcAk-rm0ZWmcaTqrKmJuOqd0Z9uGqKYgpnFWX9fhkbQlue5r1RC_Na4mvnel0oZsXdsZ23hiw8So2trMyaoYiKXV6jcsTNu67ptWt82QYLad_W6IDiG2UJ3xD6J7paq8ebg7j6J3L8-uFq_i9eZ8tThZx1qA4HE-YzPJWaIgzYQqcimoLliWQ2JSkes0SXIuWFFmeaZpDpSBLCljOSsyaZTk_Ch6PHLDV7_1xndYW69NVanGtL3HhNKUJVwG49Vo1K713pkSt87Wyt0iBRz6wWHROCwax34wSCpwaAQx9IN_-kGOgIsNMrwI2Ee7_D6vTfEXuiskGD6Nhh-2Mrf_FfqPzP1dYMcj2_rO3OzZyn3FWcITiR_enOP7y8_Lj6fL18j5L6OUvDc</recordid><startdate>200108</startdate><enddate>200108</enddate><creator>Shetty, Jagathpala</creator><creator>Diekman, Alan B.</creator><creator>Jayes, Friederike C. L.</creator><creator>Sherman, Nicholas E.</creator><creator>Naaby-Hansen, Soren</creator><creator>Flickinger, Charles J.</creator><creator>Herr, John C.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</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>200108</creationdate><title>Differential extraction and enrichment of human sperm surface proteins in a proteome: Identification of immunocontraceptive candidates</title><author>Shetty, Jagathpala ; Diekman, Alan B. ; Jayes, Friederike C. L. ; Sherman, Nicholas E. ; Naaby-Hansen, Soren ; Flickinger, Charles J. ; Herr, John C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4043-b6265327a0894adb541cd29b07e84bc877b342df9b9c1b01205f122b2d95ea533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Acrosome - chemistry</topic><topic>Adult</topic><topic>Amino Acid Sequence</topic><topic>Autoantibodies - blood</topic><topic>Autoantibodies - immunology</topic><topic>Autoantigens - analysis</topic><topic>Autoantigens - isolation & purification</topic><topic>Biotin - analogs & derivatives</topic><topic>Biotinylation</topic><topic>Blotting, Western</topic><topic>Buffers</topic><topic>Chemical Fractionation - methods</topic><topic>Contraception, Immunologic</topic><topic>Cytoskeletal Proteins - analysis</topic><topic>Cytoskeletal Proteins - isolation & purification</topic><topic>Detergents</topic><topic>Differential extraction</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Human sperm</topic><topic>Humans</topic><topic>Immunocontraception</topic><topic>Infertility, Male - blood</topic><topic>Infertility, Male - immunology</topic><topic>Isoelectric Focusing</topic><topic>Male</topic><topic>Membrane Proteins - analysis</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Molecular Sequence Data</topic><topic>Octoxynol</topic><topic>Polyethylene Glycols</topic><topic>Proteins - analysis</topic><topic>Proteins - isolation & purification</topic><topic>Proteome</topic><topic>Saline Solution, Hypertonic</topic><topic>Sequence Analysis, Protein</topic><topic>Solubility</topic><topic>Solvents</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Spermatozoa - chemistry</topic><topic>Subtraction Technique</topic><topic>Succinimides</topic><topic>Two-dimensional gel electrophoresis</topic><topic>Urea</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shetty, Jagathpala</creatorcontrib><creatorcontrib>Diekman, Alan B.</creatorcontrib><creatorcontrib>Jayes, Friederike C. L.</creatorcontrib><creatorcontrib>Sherman, Nicholas E.</creatorcontrib><creatorcontrib>Naaby-Hansen, Soren</creatorcontrib><creatorcontrib>Flickinger, Charles J.</creatorcontrib><creatorcontrib>Herr, John C.</creatorcontrib><collection>Istex</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>Electrophoresis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shetty, Jagathpala</au><au>Diekman, Alan B.</au><au>Jayes, Friederike C. L.</au><au>Sherman, Nicholas E.</au><au>Naaby-Hansen, Soren</au><au>Flickinger, Charles J.</au><au>Herr, John C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential extraction and enrichment of human sperm surface proteins in a proteome: Identification of immunocontraceptive candidates</atitle><jtitle>Electrophoresis</jtitle><addtitle>ELECTROPHORESIS</addtitle><date>2001-08</date><risdate>2001</risdate><volume>22</volume><issue>14</issue><spage>3053</spage><epage>3066</epage><pages>3053-3066</pages><issn>0173-0835</issn><eissn>1522-2683</eissn><abstract>The objective of this study was to discover previously unknown human sperm surface proteins that may be candidate contraceptive vaccinogens. To this end, methods of concentrating human sperm proteins for microsequencing by mass spectrometry were used, which increased the likelihood of identifying surface proteins. Vectorial labeling, differential extraction and two‐dimensional (2‐D) gel electrophoresis were employed to identify and isolate proteins accessible at the cell surface. Percoll harvested or swim‐up sperm were either solubilized directly or solubilized after surface labeling with sulfo‐succinimidyl‐6‐(biotinamido)hexanoate (sulfo‐NHS‐LC‐biotin). Comparisons were made of proteins extracted with four lysis buffers: (i) Celis buffer containing 9.8 M urea and 2% Igepal CA‐630; (ii) 1% Triton X (TX)‐100; (iii) 1.7% TX‐114 followed by phase partitioning; or (iv) 1 M NaCl. Blots of proteins separated by high‐resolution 2‐D electrophoresis were probed with avidin and antibodies to known proteins specific for three domains: the sperm surface (SAGA‐1), the acrosome (SP‐10), and the cytoskeleton (α‐tubulin). Celis buffer (45 min) extracted proteins from all three major compartments. However, a 20‐s extraction in Celis buffer enriched for several proteins and enabled the identification of several novel peptides by mass spectrometry. Mild extraction with TX‐100 or 1 M NaCl solubilized mainly membrane and acrosomal proteins, but not cytoskeletal proteins. Comparison of biotinylated proteins extracted by each method showed that the major vectorially labeled proteins solubilized by Celis buffer were also solubilized by TX‐100, TX‐114, and 1 M NaCl. Extraction with TX‐114 followed by phase‐partitioning significantly enriched hydrophobic surface proteins and aided resolution and isolation. Eight protein spots microsequenced following all these extraction methods proved to be novel sperm molecules.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>11565800</pmid><doi>10.1002/1522-2683(200108)22:14<3053::AID-ELPS3053>3.0.CO;2-K</doi><tpages>14</tpages></addata></record> |
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| subjects | Acrosome - chemistry Adult Amino Acid Sequence Autoantibodies - blood Autoantibodies - immunology Autoantigens - analysis Autoantigens - isolation & purification Biotin - analogs & derivatives Biotinylation Blotting, Western Buffers Chemical Fractionation - methods Contraception, Immunologic Cytoskeletal Proteins - analysis Cytoskeletal Proteins - isolation & purification Detergents Differential extraction Electrophoresis, Gel, Two-Dimensional Human sperm Humans Immunocontraception Infertility, Male - blood Infertility, Male - immunology Isoelectric Focusing Male Membrane Proteins - analysis Membrane Proteins - isolation & purification Molecular Sequence Data Octoxynol Polyethylene Glycols Proteins - analysis Proteins - isolation & purification Proteome Saline Solution, Hypertonic Sequence Analysis, Protein Solubility Solvents Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spermatozoa - chemistry Subtraction Technique Succinimides Two-dimensional gel electrophoresis Urea |
| title | Differential extraction and enrichment of human sperm surface proteins in a proteome: Identification of immunocontraceptive candidates |
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