Towards Glycoengineering in Archaea: Replacement of
            <i>Haloferax volcanii</i>
            AglD with Homologous Glycosyltransferases from Other Halophilic Archaea

Calo, Doron; Eilam, Y.; Lichtenstein, Rachel G.; Eichler, Jerry

doi:10.1128/aem.00681-10

Cited by 17 publications

(24 citation statements)

References 41 publications

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“…4C). This structure contradicts the so far valid building plan of bacterial S-layer glycans, which have been described as long-chain heteropolysaccharides composed of individual repeating units (17,18), and, thus, is reminiscent of archaeal S-layer glycans (41). Although uncommon sugar residues, such as ␣-D-FucpNAc, ␤-D-QuipNAc, or ␤-D-glycero-D-manno-Hepp are known to occur in bacterial S-layer glycans, this is the first report on an ␣-L-Fucp residue (the L-configuration was inferred from the presence of GDP-Fuc (supplemental Fig.…”

Section: Discussionmentioning

confidence: 70%

Characterization and Scope of S-layer Protein O-Glycosylation in Tannerella forsythia

Posch

Pabst

Brecker

et al. 2011

Journal of Biological Chemistry

188

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Section: Discussionmentioning

confidence: 70%

Characterization and Scope of S-layer Protein O-Glycosylation in Tannerella forsythia

Posch

Pabst

Brecker

et al. 2011

Journal of Biological Chemistry

188

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“…By replacing components of the Agl pathway with genes encoding homologous proteins from Halobacterium salinarum, Haloquadratum walsbyi or Haloarcula marismortui, Hfx. volcanii strains capable of decorating the S-layer glycoprotein with N-linked glycans distinct from the pentasaccharide normally decorating this protein were created [25,26]. At the same time, it was shown that VP4 (viral protein 4), the major structural protein of HRPV-1 (Halorubrum pleomorphic virus 1), is N-glycosylated at the same sites when expressed in either the native host, Halorubrum sp.…”

Section: Hfx Volcanii As a Glyco-engineering Platformmentioning

confidence: 98%

Add salt, add sugar: N-glycosylation in Haloferax volcanii

Kaminski

Naparstek

Kandiba

et al. 2013

Biochemical Society Transactions

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Although performed by members of all three domains of life, the archaeal version of N-glycosylation remains the least understood. Studies on Haloferax volcanii have, however, begun to correct this situation. A combination of bioinformatics, molecular biology, biochemical and mass spectrometry approaches have served to delineate the Agl pathway responsible for N-glycosylation of the S-layer glycoprotein, a reporter of this post-translational modification in Hfx. volcanii. More recently, differential N-glycosylation of the S-layer glycoprotein as a function of environmental salinity was demonstrated, showing that this post-translational modification serves an adaptive role in Hfx. volcanii. Furthermore, manipulation of the Agl pathway, together with the capability of Hfx. volcanii to N-glycosylate non-native proteins, forms the basis for establishing this species as a glyco-engineering platform. In the present review, these and other recent findings are addressed.

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“…Defining the limits of AglB promiscuity may find practical application in on-going efforts aimed at exploiting Hfx. volcanii as a platform for glycoengineering (44,45).…”

Section: Discussionmentioning

confidence: 99%

Substrate Promiscuity: AglB, the Archaeal Oligosaccharyltransferase, Can Process a Variety of Lipid-Linked Glycans

Cohen-Rosenzweig

Guan

Shaanan

et al. 2014

Appl Environ Microbiol

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bAcross evolution, N-glycosylation involves oligosaccharyltransferases that transfer lipid-linked glycans to selected Asn residues of target proteins. While these enzymes catalyze similar reactions in each domain, differences exist in terms of the chemical composition, length and degree of phosphorylation of the lipid glycan carrier, the sugar linking the glycan to the lipid carrier, and the composition and structure of the transferred glycan. To gain insight into how oligosaccharyltransferases cope with such substrate diversity, the present study analyzed the archaeal oligosaccharyltransferase AglB from four haloarchaeal species. Accordingly, it was shown that despite processing distinct lipid-linked glycans in their native hosts, AglB from Haloarcula marismortui, Halobacterium salinarum, and Haloferax mediterranei could readily replace their counterpart from Haloferax volcanii when introduced into Hfx. volcanii cells deleted of aglB. As the four enzymes show significant sequence and apparently structural homology, it appears that the functional similarity of the four AglB proteins reflects the relaxed substrate specificity of these enzymes. Such demonstration of AglB substrate promiscuity is important not only for better understanding of N-glycosylation in Archaea and elsewhere but also for efforts aimed at transforming Hfx. volcanii into a glycoengineering platform. N-glycosylation is a posttranslational modification that occurs in all three domains of life. In each case, a core or fully assembled glycan is assembled on a phosphorylated polyprenol lipid carrier, namely, dolichol in Eukarya and Archaea and undecaprenol in Bacteria, and transferred to select Asn residues of a target protein by the actions of an oligosaccharyltransferase (OST) (1-4). In higher Eukarya, the OST is a multisubunit complex, with the Stt3 (staurosporine-and temperature-sensitive) protein serving as the catalytic subunit (5, 6). In Bacteria and Archaea, the OST comprises a single subunit, namely, the Stt3 homologues PglB and AglB, respectively (7,8).While members of all three domains perform N-glycosylation, the diversity presented by the N-linked glycans added to target proteins varies greatly across evolution. In particular, the Nlinked glycans that decorate archaeal glycoproteins offer a degree of architectural and compositional variability not seen in either their bacterial or eukaryal counterparts (4, 9). Archaeal N-glycosylation also presents diversity at the level of the glycan-charged lipid carrier, with both dolichol phosphate (DolP) and dolichol pyrophosphate (DolPP) reportedly serving this role (10-15). Moreover, archaeal N-glycosylation relies on several different sugars to provide the link between the oligosaccharide and either the lipid carrier or target protein Asn residues (4). As such, the archaeal OST must cope with a degree of substrate variety not encountered by either its eukaryal or bacterial homologues. Finally, while the presence of a sequon (the motif Asn-X-Ser/Thr, where X is any residue but proline) is requi...

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Towards Glycoengineering in Archaea: Replacement of Haloferax volcanii AglD with Homologous Glycosyltransferases from Other Halophilic Archaea

Cited by 17 publications

References 41 publications

Characterization and Scope of S-layer Protein O-Glycosylation in Tannerella forsythia

Characterization and Scope of S-layer Protein O-Glycosylation in Tannerella forsythia

Add salt, add sugar: N-glycosylation in Haloferax volcanii

Substrate Promiscuity: AglB, the Archaeal Oligosaccharyltransferase, Can Process a Variety of Lipid-Linked Glycans

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