Exploring lectin-like activity of the S-layer protein of Lactobacillus acidophilus ATCC 4356
The surface layer (S-layer) protein of Lactobacillus acidophilus is a crystalline array of self-assembling, proteinaceous subunits non-covalently bound to the outmost bacterial cell wall envelope and is involved in the adherence of bacteria to host cells. We have previously described that the S-laye...
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creator | Fina Martin, Joaquina Palomino, Maria Mercedes Cutine, Anabella M. Modenutti, Carlos P. Fernández Do Porto, Dario A. Allievi, Mariana C. Zanini, Sofia H. Mariño, Karina V. Barquero, Andrea A. Ruzal, Sandra M. |
description | The surface layer (S-layer) protein of
Lactobacillus acidophilus
is a crystalline array of self-assembling, proteinaceous subunits non-covalently bound to the outmost bacterial cell wall envelope and is involved in the adherence of bacteria to host cells. We have previously described that the S-layer protein of
L. acidophilus
possesses anti-viral and anti-bacterial properties. In this work, we extracted and purified S-layer proteins from
L. acidophilus
ATCC 4356 cells to study their interaction with cell wall components from prokaryotic (i.e., peptidoglycan and lipoteichoic acids) and eukaryotic origin (i.e., mucin and chitin), as well as with viruses, bacteria, yeast, and blood cells. Using chimeric S-layer fused to green fluorescent protein (GFP) from different parts of the protein, we analyzed their binding capacity. Our results show that the C-terminal part of the S-layer protein presents lectin-like activity, interacting with different glycoepitopes. We further demonstrate that lipoteichoic acid (LTA) serves as an anchor for the S-layer protein. Finally, a structure for the C-terminal part of S-layer and possible binding sites were predicted by a homology-based model. |
doi_str_mv | 10.1007/s00253-019-09795-y |
format | Article |
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Lactobacillus acidophilus
is a crystalline array of self-assembling, proteinaceous subunits non-covalently bound to the outmost bacterial cell wall envelope and is involved in the adherence of bacteria to host cells. We have previously described that the S-layer protein of
L. acidophilus
possesses anti-viral and anti-bacterial properties. In this work, we extracted and purified S-layer proteins from
L. acidophilus
ATCC 4356 cells to study their interaction with cell wall components from prokaryotic (i.e., peptidoglycan and lipoteichoic acids) and eukaryotic origin (i.e., mucin and chitin), as well as with viruses, bacteria, yeast, and blood cells. Using chimeric S-layer fused to green fluorescent protein (GFP) from different parts of the protein, we analyzed their binding capacity. Our results show that the C-terminal part of the S-layer protein presents lectin-like activity, interacting with different glycoepitopes. We further demonstrate that lipoteichoic acid (LTA) serves as an anchor for the S-layer protein. Finally, a structure for the C-terminal part of S-layer and possible binding sites were predicted by a homology-based model.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-019-09795-y</identifier><identifier>PMID: 31053916</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Antiviral agents ; Bacteria ; Bacterial Adhesion ; Bacterial proteins ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Binding Sites ; Biomedical and Life Sciences ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; Blood cells ; Cell walls ; Chitin ; Fluorescence ; Green fluorescent protein ; Green Fluorescent Proteins - genetics ; Homology ; Lactobacillus acidophilus ; Lactobacillus acidophilus - metabolism ; Lectins - metabolism ; Life Sciences ; Lipoteichoic acid ; Membrane Glycoproteins - isolation & purification ; Membrane Glycoproteins - metabolism ; Microbial Genetics and Genomics ; Microbiology ; Mucin ; Peptidoglycans ; Physiological aspects ; Protein Binding ; Protein structure ; Proteins ; Surface layers ; Yeast ; Yeasts ; Yogurt</subject><ispartof>Applied microbiology and biotechnology, 2019-06, Vol.103 (12), p.4839-4857</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2019</rights><rights>COPYRIGHT 2019 Springer</rights><rights>Applied Microbiology and Biotechnology is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-b0175a9586f23117da8be92d343460878d1ffb9128f6896a0370d7df10590f43</citedby><cites>FETCH-LOGICAL-c440t-b0175a9586f23117da8be92d343460878d1ffb9128f6896a0370d7df10590f43</cites><orcidid>0000-0001-6388-7567</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/s00253-019-09795-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-019-09795-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31053916$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fina Martin, Joaquina</creatorcontrib><creatorcontrib>Palomino, Maria Mercedes</creatorcontrib><creatorcontrib>Cutine, Anabella M.</creatorcontrib><creatorcontrib>Modenutti, Carlos P.</creatorcontrib><creatorcontrib>Fernández Do Porto, Dario A.</creatorcontrib><creatorcontrib>Allievi, Mariana C.</creatorcontrib><creatorcontrib>Zanini, Sofia H.</creatorcontrib><creatorcontrib>Mariño, Karina V.</creatorcontrib><creatorcontrib>Barquero, Andrea A.</creatorcontrib><creatorcontrib>Ruzal, Sandra M.</creatorcontrib><title>Exploring lectin-like activity of the S-layer protein of Lactobacillus acidophilus ATCC 4356</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>The surface layer (S-layer) protein of
Lactobacillus acidophilus
is a crystalline array of self-assembling, proteinaceous subunits non-covalently bound to the outmost bacterial cell wall envelope and is involved in the adherence of bacteria to host cells. We have previously described that the S-layer protein of
L. acidophilus
possesses anti-viral and anti-bacterial properties. In this work, we extracted and purified S-layer proteins from
L. acidophilus
ATCC 4356 cells to study their interaction with cell wall components from prokaryotic (i.e., peptidoglycan and lipoteichoic acids) and eukaryotic origin (i.e., mucin and chitin), as well as with viruses, bacteria, yeast, and blood cells. Using chimeric S-layer fused to green fluorescent protein (GFP) from different parts of the protein, we analyzed their binding capacity. Our results show that the C-terminal part of the S-layer protein presents lectin-like activity, interacting with different glycoepitopes. We further demonstrate that lipoteichoic acid (LTA) serves as an anchor for the S-layer protein. Finally, a structure for the C-terminal part of S-layer and possible binding sites were predicted by a homology-based model.</description><subject>Antiviral agents</subject><subject>Bacteria</subject><subject>Bacterial Adhesion</subject><subject>Bacterial proteins</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Blood cells</subject><subject>Cell walls</subject><subject>Chitin</subject><subject>Fluorescence</subject><subject>Green fluorescent protein</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Homology</subject><subject>Lactobacillus acidophilus</subject><subject>Lactobacillus acidophilus - metabolism</subject><subject>Lectins - metabolism</subject><subject>Life Sciences</subject><subject>Lipoteichoic acid</subject><subject>Membrane Glycoproteins - isolation & purification</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mucin</subject><subject>Peptidoglycans</subject><subject>Physiological aspects</subject><subject>Protein Binding</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Surface layers</subject><subject>Yeast</subject><subject>Yeasts</subject><subject>Yogurt</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kc1q3DAUhUVpaKZJX6CLYuimGzVXP5as5TCkPzDQRWcZELItJUo1livZoX77ypm0gS660kV89_BdDkJvCXwkAPIqA9CaYSAKg5KqxssLtCGcUQyC8JdoA0TWWNaqOUevc74HILQR4hU6ZwRqpojYoJvrX2OIyQ-3VbDd5Acc_A9bmTI--GmpoqumO1t9x8EsNlVjipP1w_q9L0xsTedDmHNZ8H0c7_w6bw-7XcVZLS7RmTMh2zdP7wU6fLo-7L7g_bfPX3fbPe44hwm3q6dRdSMcZYTI3jStVbRnnHEBjWx64lyrirwTjRIGmIRe9q4cocBxdoE-nGKL3c_Z5kkffe5sCGawcc6aUqooa1QtC_r-H_Q-zmkocoUiinGQwJ-pWxOs9oOLUzLdGqq3xVIxwh6z6InqUsw5WafH5I8mLZqAXgvSp4J0KUg_FqSXsvTuSWBuj7b_u_KnkQKwE5DHtRWbng3_E_sbM4CYZQ</recordid><startdate>20190601</startdate><enddate>20190601</enddate><creator>Fina Martin, Joaquina</creator><creator>Palomino, Maria Mercedes</creator><creator>Cutine, Anabella 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lectin-like activity of the S-layer protein of Lactobacillus acidophilus ATCC 4356</title><author>Fina Martin, Joaquina ; Palomino, Maria Mercedes ; Cutine, Anabella M. ; Modenutti, Carlos P. ; Fernández Do Porto, Dario A. ; Allievi, Mariana C. ; Zanini, Sofia H. ; Mariño, Karina V. ; Barquero, Andrea A. ; Ruzal, Sandra M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-b0175a9586f23117da8be92d343460878d1ffb9128f6896a0370d7df10590f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Antiviral agents</topic><topic>Bacteria</topic><topic>Bacterial Adhesion</topic><topic>Bacterial proteins</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>Blood cells</topic><topic>Cell walls</topic><topic>Chitin</topic><topic>Fluorescence</topic><topic>Green fluorescent protein</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Homology</topic><topic>Lactobacillus acidophilus</topic><topic>Lactobacillus acidophilus - metabolism</topic><topic>Lectins - metabolism</topic><topic>Life Sciences</topic><topic>Lipoteichoic acid</topic><topic>Membrane Glycoproteins - isolation & purification</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Mucin</topic><topic>Peptidoglycans</topic><topic>Physiological aspects</topic><topic>Protein Binding</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Surface layers</topic><topic>Yeast</topic><topic>Yeasts</topic><topic>Yogurt</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fina Martin, Joaquina</creatorcontrib><creatorcontrib>Palomino, Maria 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Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2019-06-01</date><risdate>2019</risdate><volume>103</volume><issue>12</issue><spage>4839</spage><epage>4857</epage><pages>4839-4857</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>The surface layer (S-layer) protein of
Lactobacillus acidophilus
is a crystalline array of self-assembling, proteinaceous subunits non-covalently bound to the outmost bacterial cell wall envelope and is involved in the adherence of bacteria to host cells. We have previously described that the S-layer protein of
L. acidophilus
possesses anti-viral and anti-bacterial properties. In this work, we extracted and purified S-layer proteins from
L. acidophilus
ATCC 4356 cells to study their interaction with cell wall components from prokaryotic (i.e., peptidoglycan and lipoteichoic acids) and eukaryotic origin (i.e., mucin and chitin), as well as with viruses, bacteria, yeast, and blood cells. Using chimeric S-layer fused to green fluorescent protein (GFP) from different parts of the protein, we analyzed their binding capacity. Our results show that the C-terminal part of the S-layer protein presents lectin-like activity, interacting with different glycoepitopes. We further demonstrate that lipoteichoic acid (LTA) serves as an anchor for the S-layer protein. Finally, a structure for the C-terminal part of S-layer and possible binding sites were predicted by a homology-based model.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>31053916</pmid><doi>10.1007/s00253-019-09795-y</doi><tpages>19</tpages><orcidid>https://orcid.org/0000-0001-6388-7567</orcidid><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Springer Nature - Complete Springer Journals |
subjects | Antiviral agents Bacteria Bacterial Adhesion Bacterial proteins Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Blood cells Cell walls Chitin Fluorescence Green fluorescent protein Green Fluorescent Proteins - genetics Homology Lactobacillus acidophilus Lactobacillus acidophilus - metabolism Lectins - metabolism Life Sciences Lipoteichoic acid Membrane Glycoproteins - isolation & purification Membrane Glycoproteins - metabolism Microbial Genetics and Genomics Microbiology Mucin Peptidoglycans Physiological aspects Protein Binding Protein structure Proteins Surface layers Yeast Yeasts Yogurt |
title | Exploring lectin-like activity of the S-layer protein of Lactobacillus acidophilus ATCC 4356 |
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