Another cat and mouse game: Deciphering the evolution of the SCGB superfamily and exploring the molecular similarity of major cat allergen Fel d 1 and mouse ABP using computational approaches
The mammalian secretoglobin (SCGB) superfamily contains functionally diverse members, among which the major cat allergen Fel d 1 and mouse salivary androgen-binding protein (ABP) display similar subunits. We searched for molecular similarities between Fel d 1 and ABP to examine the possibility that...
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| description | The mammalian secretoglobin (SCGB) superfamily contains functionally diverse members, among which the major cat allergen Fel d 1 and mouse salivary androgen-binding protein (ABP) display similar subunits. We searched for molecular similarities between Fel d 1 and ABP to examine the possibility that they play similar roles. We aimed to i) cluster the evolutionary relationships of the SCGB superfamily; ii) identify divergence patterns, structural overlap, and protein-protein docking between Fel d 1 and ABP dimers; and iii) explore the residual interaction between ABP dimers and steroid binding in chemical communication using computational approaches. We also report that the evolutionary tree of the SCGB superfamily comprises seven unique palm-like clusters, showing the evolutionary pattern and divergence time tree of Fel d 1 with 28 ABP paralogs. Three ABP subunits (A27, BG27, and BG26) share phylogenetic relationships with Fel d 1 chains. The Fel d 1 and ABP subunits show similarities in terms of sequence conservation, identical motifs and binding site clefts. Topologically equivalent positions were visualized through superimposition of ABP A27:BG27 (AB) and ABP A27:BG26 (AG) dimers on a heterodimeric Fel d 1 model. In docking, Fel d 1-ABP dimers exhibit the maximum surface binding ability of AG compared with that of AB dimers and the several polar interactions between ABP dimers with steroids. Hence, cat Fel d 1 is an ABP-like molecule in which monomeric chains 1 and 2 are the equivalent of the ABPA and ABPBG monomers, respectively. These findings suggest that the biological and molecular function of Fel d 1 is similar to that of ABP in chemical communication, possibly via pheromone and/or steroid binding. |
| doi_str_mv | 10.1371/journal.pone.0197618 |
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We searched for molecular similarities between Fel d 1 and ABP to examine the possibility that they play similar roles. We aimed to i) cluster the evolutionary relationships of the SCGB superfamily; ii) identify divergence patterns, structural overlap, and protein-protein docking between Fel d 1 and ABP dimers; and iii) explore the residual interaction between ABP dimers and steroid binding in chemical communication using computational approaches. We also report that the evolutionary tree of the SCGB superfamily comprises seven unique palm-like clusters, showing the evolutionary pattern and divergence time tree of Fel d 1 with 28 ABP paralogs. Three ABP subunits (A27, BG27, and BG26) share phylogenetic relationships with Fel d 1 chains. The Fel d 1 and ABP subunits show similarities in terms of sequence conservation, identical motifs and binding site clefts. Topologically equivalent positions were visualized through superimposition of ABP A27:BG27 (AB) and ABP A27:BG26 (AG) dimers on a heterodimeric Fel d 1 model. In docking, Fel d 1-ABP dimers exhibit the maximum surface binding ability of AG compared with that of AB dimers and the several polar interactions between ABP dimers with steroids. Hence, cat Fel d 1 is an ABP-like molecule in which monomeric chains 1 and 2 are the equivalent of the ABPA and ABPBG monomers, respectively. These findings suggest that the biological and molecular function of Fel d 1 is similar to that of ABP in chemical communication, possibly via pheromone and/or steroid binding.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0197618</identifier><identifier>PMID: 29771985</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acids ; Allergens ; Allergens - chemistry ; Allergens - genetics ; Allergies ; Amino Acid Sequence ; Analogies ; Analysis ; Androgen-Binding Protein - chemistry ; Androgen-Binding Protein - genetics ; Androgens ; Animals ; Binding proteins ; Binding sites ; Bioinformatics ; Biology and Life Sciences ; Carrier Proteins - chemistry ; Cats ; Cats - genetics ; Chains ; Chemical communication ; Communication ; Computation ; Computational Biology ; Computer and Information Sciences ; Computer applications ; Computer Simulation ; Conservation ; Conserved sequence ; Dihydrotestosterone - chemistry ; Dimers ; Divergence ; Docking ; Equivalence ; Evolution ; Evolution, Molecular ; Genes ; Genetic aspects ; Glycoproteins - chemistry ; Glycoproteins - genetics ; Hydrophobic and Hydrophilic Interactions ; Intercellular Signaling Peptides and Proteins ; Mice - genetics ; Models, Chemical ; Molecular chains ; Molecular Docking Simulation ; Molecular evolution ; Monomers ; Mouse devices ; Multigene Family ; Pheromones ; Phylogeny ; Physical sciences ; Physiological aspects ; Physiology ; Progesterone - chemistry ; Prostate ; Proteins ; Research and Analysis Methods ; Sequence Alignment ; Sequence Homology, Amino Acid ; Steroid hormones ; Steroids ; Structure ; Structure-Activity Relationship ; Superposition (mathematics) ; Testosterone - chemistry ; Trees</subject><ispartof>PloS one, 2018-05, Vol.13 (5), p.e0197618-e0197618</ispartof><rights>COPYRIGHT 2018 Public Library of Science</rights><rights>2018 Durairaj et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2018 Durairaj et al 2018 Durairaj et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-f33bfcfa0c63b6a98a35f55246258eb6e819c55c85d9faf9f24c7601415ad34d3</citedby><cites>FETCH-LOGICAL-c692t-f33bfcfa0c63b6a98a35f55246258eb6e819c55c85d9faf9f24c7601415ad34d3</cites><orcidid>0000-0002-3807-4174</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5957422/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5957422/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,861,882,2096,2915,23847,27905,27906,53772,53774,79349,79350</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29771985$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Matsunami, Hiroaki</contributor><creatorcontrib>Durairaj, Rajesh</creatorcontrib><creatorcontrib>Pageat, Patrick</creatorcontrib><creatorcontrib>Bienboire-Frosini, Cécile</creatorcontrib><title>Another cat and mouse game: Deciphering the evolution of the SCGB superfamily and exploring the molecular similarity of major cat allergen Fel d 1 and mouse ABP using computational approaches</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The mammalian secretoglobin (SCGB) superfamily contains functionally diverse members, among which the major cat allergen Fel d 1 and mouse salivary androgen-binding protein (ABP) display similar subunits. We searched for molecular similarities between Fel d 1 and ABP to examine the possibility that they play similar roles. We aimed to i) cluster the evolutionary relationships of the SCGB superfamily; ii) identify divergence patterns, structural overlap, and protein-protein docking between Fel d 1 and ABP dimers; and iii) explore the residual interaction between ABP dimers and steroid binding in chemical communication using computational approaches. We also report that the evolutionary tree of the SCGB superfamily comprises seven unique palm-like clusters, showing the evolutionary pattern and divergence time tree of Fel d 1 with 28 ABP paralogs. Three ABP subunits (A27, BG27, and BG26) share phylogenetic relationships with Fel d 1 chains. The Fel d 1 and ABP subunits show similarities in terms of sequence conservation, identical motifs and binding site clefts. Topologically equivalent positions were visualized through superimposition of ABP A27:BG27 (AB) and ABP A27:BG26 (AG) dimers on a heterodimeric Fel d 1 model. In docking, Fel d 1-ABP dimers exhibit the maximum surface binding ability of AG compared with that of AB dimers and the several polar interactions between ABP dimers with steroids. Hence, cat Fel d 1 is an ABP-like molecule in which monomeric chains 1 and 2 are the equivalent of the ABPA and ABPBG monomers, respectively. These findings suggest that the biological and molecular function of Fel d 1 is similar to that of ABP in chemical communication, possibly via pheromone and/or steroid binding.</description><subject>Acids</subject><subject>Allergens</subject><subject>Allergens - chemistry</subject><subject>Allergens - genetics</subject><subject>Allergies</subject><subject>Amino Acid Sequence</subject><subject>Analogies</subject><subject>Analysis</subject><subject>Androgen-Binding Protein - chemistry</subject><subject>Androgen-Binding Protein - genetics</subject><subject>Androgens</subject><subject>Animals</subject><subject>Binding proteins</subject><subject>Binding sites</subject><subject>Bioinformatics</subject><subject>Biology and Life Sciences</subject><subject>Carrier Proteins - chemistry</subject><subject>Cats</subject><subject>Cats - genetics</subject><subject>Chains</subject><subject>Chemical communication</subject><subject>Communication</subject><subject>Computation</subject><subject>Computational Biology</subject><subject>Computer and Information Sciences</subject><subject>Computer applications</subject><subject>Computer Simulation</subject><subject>Conservation</subject><subject>Conserved sequence</subject><subject>Dihydrotestosterone - chemistry</subject><subject>Dimers</subject><subject>Divergence</subject><subject>Docking</subject><subject>Equivalence</subject><subject>Evolution</subject><subject>Evolution, Molecular</subject><subject>Genes</subject><subject>Genetic aspects</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - genetics</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Intercellular Signaling Peptides and Proteins</subject><subject>Mice - genetics</subject><subject>Models, Chemical</subject><subject>Molecular chains</subject><subject>Molecular Docking Simulation</subject><subject>Molecular evolution</subject><subject>Monomers</subject><subject>Mouse devices</subject><subject>Multigene Family</subject><subject>Pheromones</subject><subject>Phylogeny</subject><subject>Physical sciences</subject><subject>Physiological aspects</subject><subject>Physiology</subject><subject>Progesterone - chemistry</subject><subject>Prostate</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Steroid hormones</subject><subject>Steroids</subject><subject>Structure</subject><subject>Structure-Activity Relationship</subject><subject>Superposition (mathematics)</subject><subject>Testosterone - chemistry</subject><subject>Trees</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</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><sourceid>DOA</sourceid><recordid>eNqNk8Fu1DAQhiMEoqXwBggsISE47BLHsRNzQNoWWlaqVESBqzXr2FmvnDjYSdV9Ol4Np02rXdQDipRY4-__xzPxJMlLnM4xKfCHjRt8C3beuVbNU8wLhstHySHmJJuxLCWPd9YHybMQNmlKScnY0-Qg40WBeUkPkz-L1vVr5ZGEHkFbocYNQaEaGvURfVbSdHHTtDWKEFJXzg69cS1y-iZweXJ2jMLQKa-hMXZ746CuO-vuNY2zSg4WPAomIuBNvx3lDWzclNVa5WvVolNlUYXwzjEWx9_QEEYr6Zpu6GFMDhZB13kHcq3C8-SJBhvUi-l7lPw8_fLj5Ovs_OJsebI4n0nGs36mCVlpqSGVjKwY8BII1ZRmOctoqVZMlZhLSmVJK65Bc53lsmApzjGFiuQVOUpe3_rG2oKYeh9EluZpkec0LSOxvCUqBxvRedOA3woHRtwEnK8F-N5IqwQnVapzYABU5xwkB8IoZhXPNcaa4-j1aco2rBpVSdX2Huye6f5Oa9aidleCclrkWRYN3k0G3v0eVOhFY4JU1kKrYmfHc2OWFZyN6Jt_0Ierm6gaYgGm1S7mlaOpWFDCcU7jO1LzB6j4VKoxMl5UbWJ8T_B-TxCZXl33NQwhiOXl9_9nL37ts2932LUC26_DdHnDPpjfgtK7ELzS903GqRjn7K4bYpwzMc1ZlL3a_UH3orvBIn8BTmYlmg</recordid><startdate>20180517</startdate><enddate>20180517</enddate><creator>Durairaj, Rajesh</creator><creator>Pageat, Patrick</creator><creator>Bienboire-Frosini, Cécile</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</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>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0002-3807-4174</orcidid></search><sort><creationdate>20180517</creationdate><title>Another cat and mouse game: Deciphering the evolution of the SCGB superfamily and exploring the molecular similarity of major cat allergen Fel d 1 and mouse ABP using computational approaches</title><author>Durairaj, Rajesh ; Pageat, Patrick ; Bienboire-Frosini, Cécile</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-f33bfcfa0c63b6a98a35f55246258eb6e819c55c85d9faf9f24c7601415ad34d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Acids</topic><topic>Allergens</topic><topic>Allergens - chemistry</topic><topic>Allergens - genetics</topic><topic>Allergies</topic><topic>Amino Acid Sequence</topic><topic>Analogies</topic><topic>Analysis</topic><topic>Androgen-Binding Protein - chemistry</topic><topic>Androgen-Binding Protein - genetics</topic><topic>Androgens</topic><topic>Animals</topic><topic>Binding proteins</topic><topic>Binding sites</topic><topic>Bioinformatics</topic><topic>Biology and Life Sciences</topic><topic>Carrier Proteins - chemistry</topic><topic>Cats</topic><topic>Cats - genetics</topic><topic>Chains</topic><topic>Chemical communication</topic><topic>Communication</topic><topic>Computation</topic><topic>Computational Biology</topic><topic>Computer and Information Sciences</topic><topic>Computer applications</topic><topic>Computer Simulation</topic><topic>Conservation</topic><topic>Conserved sequence</topic><topic>Dihydrotestosterone - chemistry</topic><topic>Dimers</topic><topic>Divergence</topic><topic>Docking</topic><topic>Equivalence</topic><topic>Evolution</topic><topic>Evolution, Molecular</topic><topic>Genes</topic><topic>Genetic aspects</topic><topic>Glycoproteins - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Durairaj, Rajesh</au><au>Pageat, Patrick</au><au>Bienboire-Frosini, Cécile</au><au>Matsunami, Hiroaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Another cat and mouse game: Deciphering the evolution of the SCGB superfamily and exploring the molecular similarity of major cat allergen Fel d 1 and mouse ABP using computational approaches</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2018-05-17</date><risdate>2018</risdate><volume>13</volume><issue>5</issue><spage>e0197618</spage><epage>e0197618</epage><pages>e0197618-e0197618</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The mammalian secretoglobin (SCGB) superfamily contains functionally diverse members, among which the major cat allergen Fel d 1 and mouse salivary androgen-binding protein (ABP) display similar subunits. We searched for molecular similarities between Fel d 1 and ABP to examine the possibility that they play similar roles. We aimed to i) cluster the evolutionary relationships of the SCGB superfamily; ii) identify divergence patterns, structural overlap, and protein-protein docking between Fel d 1 and ABP dimers; and iii) explore the residual interaction between ABP dimers and steroid binding in chemical communication using computational approaches. We also report that the evolutionary tree of the SCGB superfamily comprises seven unique palm-like clusters, showing the evolutionary pattern and divergence time tree of Fel d 1 with 28 ABP paralogs. Three ABP subunits (A27, BG27, and BG26) share phylogenetic relationships with Fel d 1 chains. The Fel d 1 and ABP subunits show similarities in terms of sequence conservation, identical motifs and binding site clefts. Topologically equivalent positions were visualized through superimposition of ABP A27:BG27 (AB) and ABP A27:BG26 (AG) dimers on a heterodimeric Fel d 1 model. In docking, Fel d 1-ABP dimers exhibit the maximum surface binding ability of AG compared with that of AB dimers and the several polar interactions between ABP dimers with steroids. Hence, cat Fel d 1 is an ABP-like molecule in which monomeric chains 1 and 2 are the equivalent of the ABPA and ABPBG monomers, respectively. These findings suggest that the biological and molecular function of Fel d 1 is similar to that of ABP in chemical communication, possibly via pheromone and/or steroid binding.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>29771985</pmid><doi>10.1371/journal.pone.0197618</doi><tpages>e0197618</tpages><orcidid>https://orcid.org/0000-0002-3807-4174</orcidid><oa>free_for_read</oa></addata></record> |
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| language | eng |
| recordid | cdi_plos_journals_2040744508 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Public Library of Science (PLoS); PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Acids Allergens Allergens - chemistry Allergens - genetics Allergies Amino Acid Sequence Analogies Analysis Androgen-Binding Protein - chemistry Androgen-Binding Protein - genetics Androgens Animals Binding proteins Binding sites Bioinformatics Biology and Life Sciences Carrier Proteins - chemistry Cats Cats - genetics Chains Chemical communication Communication Computation Computational Biology Computer and Information Sciences Computer applications Computer Simulation Conservation Conserved sequence Dihydrotestosterone - chemistry Dimers Divergence Docking Equivalence Evolution Evolution, Molecular Genes Genetic aspects Glycoproteins - chemistry Glycoproteins - genetics Hydrophobic and Hydrophilic Interactions Intercellular Signaling Peptides and Proteins Mice - genetics Models, Chemical Molecular chains Molecular Docking Simulation Molecular evolution Monomers Mouse devices Multigene Family Pheromones Phylogeny Physical sciences Physiological aspects Physiology Progesterone - chemistry Prostate Proteins Research and Analysis Methods Sequence Alignment Sequence Homology, Amino Acid Steroid hormones Steroids Structure Structure-Activity Relationship Superposition (mathematics) Testosterone - chemistry Trees |
| title | Another cat and mouse game: Deciphering the evolution of the SCGB superfamily and exploring the molecular similarity of major cat allergen Fel d 1 and mouse ABP using computational approaches |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T04%3A44%3A19IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Another%20cat%20and%20mouse%20game:%20Deciphering%20the%20evolution%20of%20the%20SCGB%20superfamily%20and%20exploring%20the%20molecular%20similarity%20of%20major%20cat%20allergen%20Fel%20d%201%20and%20mouse%20ABP%20using%20computational%20approaches&rft.jtitle=PloS%20one&rft.au=Durairaj,%20Rajesh&rft.date=2018-05-17&rft.volume=13&rft.issue=5&rft.spage=e0197618&rft.epage=e0197618&rft.pages=e0197618-e0197618&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0197618&rft_dat=%3Cgale_plos_%3EA539145539%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2040744508&rft_id=info:pmid/29771985&rft_galeid=A539145539&rft_doaj_id=oai_doaj_org_article_93d0f4a6aa5f49ac9a36516d94f11f91&rfr_iscdi=true |