{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T13:26:45Z","timestamp":1790515605114,"version":"4.1.0"},"reference-count":46,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2017,3,15]],"date-time":"2017-03-15T00:00:00Z","timestamp":1489536000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100003977","name":"Israel Science Foundation","doi-asserted-by":"publisher","award":["109\/16"],"award-info":[{"award-number":["109\/16"]}],"id":[{"id":"10.13039\/501100003977","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2017,3,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    N-Glycosylation, the covalent linkage of glycans to select Asn residues of target proteins, is an almost universal posttranslational modification in archaea. However, whereas roles for N-glycosylation have been defined in eukarya and bacteria, the function of archaeal N-glycosylation remains unclear. Here, the impact of perturbed N-glycosylation on the structure and physiology of the haloarchaeon\n                    <jats:named-content content-type=\"genus-species\">Haloferax volcanii<\/jats:named-content>\n                    was considered. Cryo-electron microscopy was used to examine right-side-out membrane vesicles prepared from cells of a parent strain and from strains lacking genes encoding glycosyltransferases involved in assembling the N-linked pentasaccharide decorating the surface layer (S-layer) glycoprotein, the sole component of the S-layer surrounding\n                    <jats:named-content content-type=\"genus-species\">H. volcanii<\/jats:named-content>\n                    cells. Whereas a regularly repeating S-layer covered the entire surface of vesicles prepared from parent strain cells, vesicles from the mutant cells were only partially covered. To determine whether such N-glycosylation-related effects on S-layer assembly also affected cell function, the secretion of a reporter protein was addressed in the parent and N-glycosylation mutant strains. Compromised S-layer glycoprotein N-glycosylation resulted in impaired transfer of the reporter past the S-layer and into the growth medium. Finally, an assessment of S-layer glycoprotein susceptibility to added proteases in the mutants revealed that in cells lacking AglD, which is involved in adding the final pentasaccharide sugar, a distinct S-layer glycoprotein conformation was assumed in which the N-terminal region was readily degraded. Perturbed N-glycosylation thus affects S-layer glycoprotein folding. These findings suggest that\n                    <jats:named-content content-type=\"genus-species\">H. volcanii<\/jats:named-content>\n                    could adapt to changes in its surroundings by modulating N-glycosylation so as to affect S-layer architecture and function.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>IMPORTANCE<\/jats:bold>\n                    Long held to be a process unique to eukaryotes, it is now accepted that bacteria and archaea also perform N-glycosylation, namely, the covalent attachment of sugars to select asparagine residues of target proteins. Yet, while information on the importance of N-glycosylation in eukaryotes and bacteria is available, the role of this posttranslational modification in archaea remains unclear. Here, insight into the purpose of archaeal N-glycosylation was gained by addressing the surface layer (S-layer) surrounding cells of the halophilic species\n                    <jats:named-content content-type=\"genus-species\">Haloferax volcanii<\/jats:named-content>\n                    . Relying on mutant strains defective in N-glycosylation, such efforts revealed that compromised N-glycosylation affected S-layer integrity and the transfer of a secreted reporter protein across the S-layer into the growth medium, as well as the conformation of the S-layer glycoprotein, the sole component of the S-layer. Thus, by modifying N-glycosylation,\n                    <jats:named-content content-type=\"genus-species\">H. volcanii<\/jats:named-content>\n                    cells can change how they interact with their surroundings.\n                  <\/jats:p>","DOI":"10.1128\/aem.03152-16","type":"journal-article","created":{"date-parts":[[2016,12,30]],"date-time":"2016-12-30T21:40:27Z","timestamp":1483134027000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":44,"title":["N-Glycosylation Is Important for Proper Haloferax volcanii S-Layer Stability and Function"],"prefix":"10.1128","volume":"83","author":[{"given":"Adi","family":"Tamir","sequence":"first","affiliation":[{"name":"Department of Life Sciences, Ben Gurion University of the Negev, Beersheva, Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jerry","family":"Eichler","sequence":"additional","affiliation":[{"name":"Department of Life 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