Phage display-derived antibody fragments against conserved regions of VacA toxin of Helicobacter pylori
Infection with Helicobacter pylori may result in the emergence of gastric adenocarcinoma. Among various toxins assisting pathogenesis of H. pylori , the vacuolating cytotoxin A (VacA) is one of the most potent toxins known as the major cause of the peptic ulcer and gastric adenocarcinoma. To isolate...
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| Veröffentlicht in: | Applied microbiology and biotechnology 2018-08, Vol.102 (16), p.6899-6913 |
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| creator | Fahimi, Farnaz Sarhaddi, Shamim Fouladi, Mehdi Samadi, Naser Sadeghi, Javid Golchin, Asal Tohidkia, Mohammad Reza Barar, Jaleh Omidi, Yadollah |
| description | Infection with
Helicobacter pylori
may result in the emergence of gastric adenocarcinoma. Among various toxins assisting pathogenesis of
H. pylori
, the vacuolating cytotoxin A (VacA) is one of the most potent toxins known as the major cause of the peptic ulcer and gastric adenocarcinoma. To isolate single-chain variable fragments (scFvs) against two conserved regions of VacA, we capitalized on the phage display technology and a solution-phase biopanning (SPB). Characterization of scFvs was carried out by enzyme-linked immunosorbent assay (ELISA), immunoblotting, and surface plasmon resonance (SPR). Bioinformatics analyses were also performed in order to characterize the structural and functional properties of the isolated scFvs and the interaction(s) between the isolated antibodies (Ab)-antigen (Ag). After four rounds of biopanning, the positive colonies detected by scFv ELISA were harvested to extract the plasmids and perform sequencing. Of several colonies, three colonies showed high affinity to the VacA1 and two colonies for the VacA2. Further complementary examinations (e.g., sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), western blot, SPR, and flow cytometry) displayed the high affinity and specificity of the isolated scFvs to the VacA. Docking results revealed the interaction of the complementarity-determining regions (CDRs) with the VacA peptide. In conclusion, for the first time, we report on the isolation of several scFvs against conserved residues of VacA toxin with high affinity and specificity, which may be used as novel diagnostic/therapeutic tool in the
H. pylori
infection. |
| doi_str_mv | 10.1007/s00253-018-9068-4 |
| format | Article |
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Helicobacter pylori
may result in the emergence of gastric adenocarcinoma. Among various toxins assisting pathogenesis of
H. pylori
, the vacuolating cytotoxin A (VacA) is one of the most potent toxins known as the major cause of the peptic ulcer and gastric adenocarcinoma. To isolate single-chain variable fragments (scFvs) against two conserved regions of VacA, we capitalized on the phage display technology and a solution-phase biopanning (SPB). Characterization of scFvs was carried out by enzyme-linked immunosorbent assay (ELISA), immunoblotting, and surface plasmon resonance (SPR). Bioinformatics analyses were also performed in order to characterize the structural and functional properties of the isolated scFvs and the interaction(s) between the isolated antibodies (Ab)-antigen (Ag). After four rounds of biopanning, the positive colonies detected by scFv ELISA were harvested to extract the plasmids and perform sequencing. Of several colonies, three colonies showed high affinity to the VacA1 and two colonies for the VacA2. Further complementary examinations (e.g., sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), western blot, SPR, and flow cytometry) displayed the high affinity and specificity of the isolated scFvs to the VacA. Docking results revealed the interaction of the complementarity-determining regions (CDRs) with the VacA peptide. In conclusion, for the first time, we report on the isolation of several scFvs against conserved residues of VacA toxin with high affinity and specificity, which may be used as novel diagnostic/therapeutic tool in the
H. pylori
infection.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-018-9068-4</identifier><identifier>PMID: 29862446</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Adenocarcinoma ; Affinity ; Analysis ; Antibodies ; Bacteria ; Bacteriophages ; Bioinformatics ; Biomedical and Life Sciences ; Biotechnological Products and Process Engineering ; Biotechnology ; Cancer ; Colonies ; Complementarity ; Diagnostic software ; Diagnostic systems ; Display devices ; Docking ; Electrophoresis ; Enzyme-linked immunosorbent assay ; Flow cytometry ; Fragments ; Gel electrophoresis ; Health risk assessment ; Helicobacter pylori ; Immunoblotting ; Life Sciences ; Methods ; Microbial Genetics and Genomics ; Microbiology ; Pathogenesis ; Phage display ; Phages ; Plasmids ; Sodium dodecyl sulfate ; Sodium lauryl sulfate ; Structure-function relationships ; Surface plasmon resonance ; Toxins ; Western immunoblotting</subject><ispartof>Applied microbiology and biotechnology, 2018-08, Vol.102 (16), p.6899-6913</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2018</rights><rights>COPYRIGHT 2018 Springer</rights><rights>Applied Microbiology and Biotechnology is a copyright of Springer, (2018). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c510t-8c53150b1bd1a39aea21abe28120b5f179ac412e0ae6618bdda72ba50c35b0eb3</citedby><cites>FETCH-LOGICAL-c510t-8c53150b1bd1a39aea21abe28120b5f179ac412e0ae6618bdda72ba50c35b0eb3</cites><orcidid>0000-0003-0067-2475</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-018-9068-4$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-018-9068-4$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29862446$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fahimi, Farnaz</creatorcontrib><creatorcontrib>Sarhaddi, Shamim</creatorcontrib><creatorcontrib>Fouladi, Mehdi</creatorcontrib><creatorcontrib>Samadi, Naser</creatorcontrib><creatorcontrib>Sadeghi, Javid</creatorcontrib><creatorcontrib>Golchin, Asal</creatorcontrib><creatorcontrib>Tohidkia, Mohammad Reza</creatorcontrib><creatorcontrib>Barar, Jaleh</creatorcontrib><creatorcontrib>Omidi, Yadollah</creatorcontrib><title>Phage display-derived antibody fragments against conserved regions of VacA toxin of Helicobacter pylori</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Infection with
Helicobacter pylori
may result in the emergence of gastric adenocarcinoma. Among various toxins assisting pathogenesis of
H. pylori
, the vacuolating cytotoxin A (VacA) is one of the most potent toxins known as the major cause of the peptic ulcer and gastric adenocarcinoma. To isolate single-chain variable fragments (scFvs) against two conserved regions of VacA, we capitalized on the phage display technology and a solution-phase biopanning (SPB). Characterization of scFvs was carried out by enzyme-linked immunosorbent assay (ELISA), immunoblotting, and surface plasmon resonance (SPR). Bioinformatics analyses were also performed in order to characterize the structural and functional properties of the isolated scFvs and the interaction(s) between the isolated antibodies (Ab)-antigen (Ag). After four rounds of biopanning, the positive colonies detected by scFv ELISA were harvested to extract the plasmids and perform sequencing. Of several colonies, three colonies showed high affinity to the VacA1 and two colonies for the VacA2. Further complementary examinations (e.g., sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), western blot, SPR, and flow cytometry) displayed the high affinity and specificity of the isolated scFvs to the VacA. Docking results revealed the interaction of the complementarity-determining regions (CDRs) with the VacA peptide. In conclusion, for the first time, we report on the isolation of several scFvs against conserved residues of VacA toxin with high affinity and specificity, which may be used as novel diagnostic/therapeutic tool in the
H. pylori
infection.</description><subject>Adenocarcinoma</subject><subject>Affinity</subject><subject>Analysis</subject><subject>Antibodies</subject><subject>Bacteria</subject><subject>Bacteriophages</subject><subject>Bioinformatics</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnological Products and Process Engineering</subject><subject>Biotechnology</subject><subject>Cancer</subject><subject>Colonies</subject><subject>Complementarity</subject><subject>Diagnostic software</subject><subject>Diagnostic systems</subject><subject>Display devices</subject><subject>Docking</subject><subject>Electrophoresis</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Flow cytometry</subject><subject>Fragments</subject><subject>Gel electrophoresis</subject><subject>Health risk assessment</subject><subject>Helicobacter pylori</subject><subject>Immunoblotting</subject><subject>Life Sciences</subject><subject>Methods</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Pathogenesis</subject><subject>Phage display</subject><subject>Phages</subject><subject>Plasmids</subject><subject>Sodium dodecyl sulfate</subject><subject>Sodium lauryl sulfate</subject><subject>Structure-function relationships</subject><subject>Surface plasmon resonance</subject><subject>Toxins</subject><subject>Western 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display-derived antibody fragments against conserved regions of VacA toxin of Helicobacter pylori</title><author>Fahimi, Farnaz ; Sarhaddi, Shamim ; Fouladi, Mehdi ; Samadi, Naser ; Sadeghi, Javid ; Golchin, Asal ; Tohidkia, Mohammad Reza ; Barar, Jaleh ; Omidi, Yadollah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c510t-8c53150b1bd1a39aea21abe28120b5f179ac412e0ae6618bdda72ba50c35b0eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Adenocarcinoma</topic><topic>Affinity</topic><topic>Analysis</topic><topic>Antibodies</topic><topic>Bacteria</topic><topic>Bacteriophages</topic><topic>Bioinformatics</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnological Products and Process Engineering</topic><topic>Biotechnology</topic><topic>Cancer</topic><topic>Colonies</topic><topic>Complementarity</topic><topic>Diagnostic software</topic><topic>Diagnostic systems</topic><topic>Display devices</topic><topic>Docking</topic><topic>Electrophoresis</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Flow cytometry</topic><topic>Fragments</topic><topic>Gel electrophoresis</topic><topic>Health risk assessment</topic><topic>Helicobacter pylori</topic><topic>Immunoblotting</topic><topic>Life Sciences</topic><topic>Methods</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Pathogenesis</topic><topic>Phage display</topic><topic>Phages</topic><topic>Plasmids</topic><topic>Sodium dodecyl sulfate</topic><topic>Sodium lauryl sulfate</topic><topic>Structure-function relationships</topic><topic>Surface plasmon resonance</topic><topic>Toxins</topic><topic>Western immunoblotting</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fahimi, Farnaz</creatorcontrib><creatorcontrib>Sarhaddi, Shamim</creatorcontrib><creatorcontrib>Fouladi, 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Jaleh</au><au>Omidi, Yadollah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phage display-derived antibody fragments against conserved regions of VacA toxin of Helicobacter pylori</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2018-08-01</date><risdate>2018</risdate><volume>102</volume><issue>16</issue><spage>6899</spage><epage>6913</epage><pages>6899-6913</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>Infection with
Helicobacter pylori
may result in the emergence of gastric adenocarcinoma. Among various toxins assisting pathogenesis of
H. pylori
, the vacuolating cytotoxin A (VacA) is one of the most potent toxins known as the major cause of the peptic ulcer and gastric adenocarcinoma. To isolate single-chain variable fragments (scFvs) against two conserved regions of VacA, we capitalized on the phage display technology and a solution-phase biopanning (SPB). Characterization of scFvs was carried out by enzyme-linked immunosorbent assay (ELISA), immunoblotting, and surface plasmon resonance (SPR). Bioinformatics analyses were also performed in order to characterize the structural and functional properties of the isolated scFvs and the interaction(s) between the isolated antibodies (Ab)-antigen (Ag). After four rounds of biopanning, the positive colonies detected by scFv ELISA were harvested to extract the plasmids and perform sequencing. Of several colonies, three colonies showed high affinity to the VacA1 and two colonies for the VacA2. Further complementary examinations (e.g., sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), western blot, SPR, and flow cytometry) displayed the high affinity and specificity of the isolated scFvs to the VacA. Docking results revealed the interaction of the complementarity-determining regions (CDRs) with the VacA peptide. In conclusion, for the first time, we report on the isolation of several scFvs against conserved residues of VacA toxin with high affinity and specificity, which may be used as novel diagnostic/therapeutic tool in the
H. pylori
infection.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29862446</pmid><doi>10.1007/s00253-018-9068-4</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0003-0067-2475</orcidid></addata></record> |
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| ispartof | Applied microbiology and biotechnology, 2018-08, Vol.102 (16), p.6899-6913 |
| issn | 0175-7598 1432-0614 |
| language | eng |
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| source | Springer Nature - Complete Springer Journals |
| subjects | Adenocarcinoma Affinity Analysis Antibodies Bacteria Bacteriophages Bioinformatics Biomedical and Life Sciences Biotechnological Products and Process Engineering Biotechnology Cancer Colonies Complementarity Diagnostic software Diagnostic systems Display devices Docking Electrophoresis Enzyme-linked immunosorbent assay Flow cytometry Fragments Gel electrophoresis Health risk assessment Helicobacter pylori Immunoblotting Life Sciences Methods Microbial Genetics and Genomics Microbiology Pathogenesis Phage display Phages Plasmids Sodium dodecyl sulfate Sodium lauryl sulfate Structure-function relationships Surface plasmon resonance Toxins Western immunoblotting |
| title | Phage display-derived antibody fragments against conserved regions of VacA toxin of Helicobacter pylori |
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