Glycobiology of surface layer proteins
Over the last two decades, a significant change of perception has taken place regarding prokaryotic glycoproteins. For many years, protein glycosylation was assumed to be limited to eukaryotes; but now, a wealth of information on structure, function, biosynthesis and molecular biology of prokaryotic...
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description | Over the last two decades, a significant change of perception has taken place regarding prokaryotic glycoproteins. For many years, protein glycosylation was assumed to be limited to eukaryotes; but now, a wealth of information on structure, function, biosynthesis and molecular biology of prokaryotic glycoproteins has accumulated, with surface layer (S-layer) glycoproteins being one of the best studied examples. With the designation of Archaea as a second prokaryotic domain of life, the occurrence of glycosylated S-layer proteins had been considered a taxonomic criterion for differentiation between Bacteria and Archaea. Extensive structural investigations, however, have demonstrated that S-layer glycoproteins are present in both domains. Among Gram-positive bacteria, S-layer glycoproteins have been identified only in bacilli. In Gram-negative organisms, their presence is still not fully investigated; presently, there is no indication for their existence in this class of bacteria. Extensive biochemical studies of the S-layer glycoprotein from
Halobacterium halobium have, at least in part, unravelled the glycosylation pathway in Archaea; molecular biological analyses of these pathways have not been performed, so far. Significant observations concern the occurrence of unusual linkage regions both in archaeal and bacterial S-layer glycoproteins. Regarding S-layer glycoproteins of bacteria, first genetic data have shed some light into the molecular organization of the glycosylation machinery in this domain. In addition to basic S-layer glycoprotein research, the biotechnological application potential of these molecules has been explored. With the development of staightforward molecular biological methods, fascinating possibilities for the expression of prokaryotic glycoproteins will become available. S-layer glycoprotein research has opened up opportunities for the production of recombinant glycosylation enzymes and tailor-made S-layer glycoproteins in large quantities, which are commercially not yet available. These bacterial systems may provide economic technologies for the production of biotechnologically and medically important glycan structures in the future. |
doi_str_mv | 10.1016/S0300-9084(01)01299-8 |
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Halobacterium halobium have, at least in part, unravelled the glycosylation pathway in Archaea; molecular biological analyses of these pathways have not been performed, so far. Significant observations concern the occurrence of unusual linkage regions both in archaeal and bacterial S-layer glycoproteins. Regarding S-layer glycoproteins of bacteria, first genetic data have shed some light into the molecular organization of the glycosylation machinery in this domain. In addition to basic S-layer glycoprotein research, the biotechnological application potential of these molecules has been explored. With the development of staightforward molecular biological methods, fascinating possibilities for the expression of prokaryotic glycoproteins will become available. S-layer glycoprotein research has opened up opportunities for the production of recombinant glycosylation enzymes and tailor-made S-layer glycoproteins in large quantities, which are commercially not yet available. These bacterial systems may provide economic technologies for the production of biotechnologically and medically important glycan structures in the future.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/S0300-9084(01)01299-8</identifier><identifier>PMID: 11522387</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>application potential ; Archaea ; Archaeal Proteins - chemistry ; Archaeal Proteins - ultrastructure ; Bacillus - chemistry ; Bacillus - classification ; Bacillus - ultrastructure ; bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Bacterial Proteins - ultrastructure ; Biotechnology ; Freeze Etching ; Glycosylation ; Gram-Negative Bacteria - chemistry ; Halobacterium halobium ; Halobacterium salinarum - chemistry ; Halobacterium salinarum - ultrastructure ; Membrane Glycoproteins - chemistry ; Membrane Glycoproteins - metabolism ; Membrane Glycoproteins - ultrastructure ; Polysaccharides - chemistry ; Prokaryotic Cells ; surface-layer (S-layer) glycoproteins</subject><ispartof>Biochimie, 2001-07, Vol.83 (7), p.591-599</ispartof><rights>2001 Société française de biochimie et biologie moléculaire / Éditions scientifiques et médicales Elsevier SAS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-4b84e5e2d2ade77866480def4673550b7c37ebefd4520b0ba86493770bf2c4383</citedby><cites>FETCH-LOGICAL-c392t-4b84e5e2d2ade77866480def4673550b7c37ebefd4520b0ba86493770bf2c4383</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0300-9084(01)01299-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11522387$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schäffer, Christina</creatorcontrib><creatorcontrib>Messner, Paul</creatorcontrib><title>Glycobiology of surface layer proteins</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>Over the last two decades, a significant change of perception has taken place regarding prokaryotic glycoproteins. For many years, protein glycosylation was assumed to be limited to eukaryotes; but now, a wealth of information on structure, function, biosynthesis and molecular biology of prokaryotic glycoproteins has accumulated, with surface layer (S-layer) glycoproteins being one of the best studied examples. With the designation of Archaea as a second prokaryotic domain of life, the occurrence of glycosylated S-layer proteins had been considered a taxonomic criterion for differentiation between Bacteria and Archaea. Extensive structural investigations, however, have demonstrated that S-layer glycoproteins are present in both domains. Among Gram-positive bacteria, S-layer glycoproteins have been identified only in bacilli. In Gram-negative organisms, their presence is still not fully investigated; presently, there is no indication for their existence in this class of bacteria. Extensive biochemical studies of the S-layer glycoprotein from
Halobacterium halobium have, at least in part, unravelled the glycosylation pathway in Archaea; molecular biological analyses of these pathways have not been performed, so far. Significant observations concern the occurrence of unusual linkage regions both in archaeal and bacterial S-layer glycoproteins. Regarding S-layer glycoproteins of bacteria, first genetic data have shed some light into the molecular organization of the glycosylation machinery in this domain. In addition to basic S-layer glycoprotein research, the biotechnological application potential of these molecules has been explored. With the development of staightforward molecular biological methods, fascinating possibilities for the expression of prokaryotic glycoproteins will become available. S-layer glycoprotein research has opened up opportunities for the production of recombinant glycosylation enzymes and tailor-made S-layer glycoproteins in large quantities, which are commercially not yet available. These bacterial systems may provide economic technologies for the production of biotechnologically and medically important glycan structures in the future.</description><subject>application potential</subject><subject>Archaea</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - ultrastructure</subject><subject>Bacillus - chemistry</subject><subject>Bacillus - classification</subject><subject>Bacillus - ultrastructure</subject><subject>bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacterial Proteins - ultrastructure</subject><subject>Biotechnology</subject><subject>Freeze Etching</subject><subject>Glycosylation</subject><subject>Gram-Negative Bacteria - chemistry</subject><subject>Halobacterium halobium</subject><subject>Halobacterium salinarum - chemistry</subject><subject>Halobacterium salinarum - ultrastructure</subject><subject>Membrane Glycoproteins - chemistry</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Membrane Glycoproteins - ultrastructure</subject><subject>Polysaccharides - chemistry</subject><subject>Prokaryotic Cells</subject><subject>surface-layer (S-layer) glycoproteins</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQQC0EoqXwE0CZKhgC54_YzoRQBQWpEgMwW7FzQUFpXewEKf-e9EMwdrrl3b3TI-SSwi0FKu_egAOkOWhxDfQGKMvzVB-RMZVcp5JqfkzGf8iInMX4BQAZsPyUjCjNGONajcl03vTO29o3_rNPfJXELlSFw6QpegzJOvgW61U8JydV0US82M8J-Xh6fJ89p4vX-cvsYZE6nrM2FVYLzJCVrChRKS2l0FBiJaTiWQZWOa7QYlWKjIEFW2gpcq4U2Io5wTWfkOnu7iD-7jC2ZllHh01TrNB30ShKGWeKHwRprvRAygHMdqALPsaAlVmHelmE3lAwm5JmW9JsMhmgZlvSbD652gs6u8Tyf2ufbgDudwAOPX5qDCa6GlcOyzqga03p6wOKX6rfgQ8</recordid><startdate>20010701</startdate><enddate>20010701</enddate><creator>Schäffer, Christina</creator><creator>Messner, Paul</creator><general>Elsevier Masson SAS</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20010701</creationdate><title>Glycobiology of surface layer proteins</title><author>Schäffer, Christina ; Messner, Paul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-4b84e5e2d2ade77866480def4673550b7c37ebefd4520b0ba86493770bf2c4383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>application potential</topic><topic>Archaea</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - ultrastructure</topic><topic>Bacillus - chemistry</topic><topic>Bacillus - classification</topic><topic>Bacillus - ultrastructure</topic><topic>bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacterial Proteins - ultrastructure</topic><topic>Biotechnology</topic><topic>Freeze Etching</topic><topic>Glycosylation</topic><topic>Gram-Negative Bacteria - chemistry</topic><topic>Halobacterium halobium</topic><topic>Halobacterium salinarum - chemistry</topic><topic>Halobacterium salinarum - ultrastructure</topic><topic>Membrane Glycoproteins - chemistry</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Membrane Glycoproteins - ultrastructure</topic><topic>Polysaccharides - chemistry</topic><topic>Prokaryotic Cells</topic><topic>surface-layer (S-layer) glycoproteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schäffer, Christina</creatorcontrib><creatorcontrib>Messner, Paul</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schäffer, Christina</au><au>Messner, Paul</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycobiology of surface layer proteins</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>2001-07-01</date><risdate>2001</risdate><volume>83</volume><issue>7</issue><spage>591</spage><epage>599</epage><pages>591-599</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>Over the last two decades, a significant change of perception has taken place regarding prokaryotic glycoproteins. 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Halobacterium halobium have, at least in part, unravelled the glycosylation pathway in Archaea; molecular biological analyses of these pathways have not been performed, so far. Significant observations concern the occurrence of unusual linkage regions both in archaeal and bacterial S-layer glycoproteins. Regarding S-layer glycoproteins of bacteria, first genetic data have shed some light into the molecular organization of the glycosylation machinery in this domain. In addition to basic S-layer glycoprotein research, the biotechnological application potential of these molecules has been explored. With the development of staightforward molecular biological methods, fascinating possibilities for the expression of prokaryotic glycoproteins will become available. S-layer glycoprotein research has opened up opportunities for the production of recombinant glycosylation enzymes and tailor-made S-layer glycoproteins in large quantities, which are commercially not yet available. These bacterial systems may provide economic technologies for the production of biotechnologically and medically important glycan structures in the future.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>11522387</pmid><doi>10.1016/S0300-9084(01)01299-8</doi><tpages>9</tpages></addata></record> |
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subjects | application potential Archaea Archaeal Proteins - chemistry Archaeal Proteins - ultrastructure Bacillus - chemistry Bacillus - classification Bacillus - ultrastructure bacteria Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacterial Proteins - ultrastructure Biotechnology Freeze Etching Glycosylation Gram-Negative Bacteria - chemistry Halobacterium halobium Halobacterium salinarum - chemistry Halobacterium salinarum - ultrastructure Membrane Glycoproteins - chemistry Membrane Glycoproteins - metabolism Membrane Glycoproteins - ultrastructure Polysaccharides - chemistry Prokaryotic Cells surface-layer (S-layer) glycoproteins |
title | Glycobiology of surface layer proteins |
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