Chapter 25 : -Linked Protein Glycosylation in

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-linked protein glycosylation is the most common type of protein modification in eukaryotes and is the topic of this chapter. The chapter demonstrates that the glycome is an excellent toolbox for glycobiologists to understand the fundamentals of this pathway, to develop new techniques for glycobiology, and to exploit this pathway for novel diagnostics and therapeutics. A section summarizes the -linked proteins identified so far and provides further information on the roles for the posttranslational modification in which involves in cellular function. The importance of CjaA for the in vivo survival of has recently been shown in chicken colonization studies: birds immunized with an avirulent strain of expressing plasmid-borne showed reduced colonization. In addition, gene clusters corresponding to the -linked protein glycosylation pathway were shown to be present in various isolates of , RM2100, RM3195, subsp. 269.97, RM2228, ATCC BAA-381, 525.92, 13826, and subsp. 82-40, demonstrating that this pathway and potentially the bacillosamine-containing heptasaccharide are conserved among all species. provides researchers with an excellent model system because this organism has both well-characterized -linked and -linked protein glycosylation systems.

Citation: Nothaft H, Amber S, Aebi M, Szymanski C. 2008. -Linked Protein Glycosylation in , p 447-469. In Nachamkin I, Szymanski C, Blaser M (ed), , Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815554.ch25
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Image of Figure 1.
Figure 1.

Schematic pathway of -linked protein glycosylation at the plasma membrane of . The assembly of a heptasaccharide takes place on the lipid bactoprenylpyrophosphate at the cytoplasmic side of the membrane by the glycosyltransferases PglC, PglA, PglJ, PglH, and PglI. UDP-bacillosamine is synthesized from UDP-GlcNAc by PglF, PglE, and PglD. The ABC-transporter PglK mediates the translocation of the lipid-linked heptasaccharide across the membrane. The oligosaccharyltransferase catalyzes the transfer of the heptasaccharide from the lipid carrier to selected asparagine residues on nascent polypeptide chains. This pathway is encoded by the operon shown below, with the gene encoding the oligosaccharyltransferase highlighted.

Citation: Nothaft H, Amber S, Aebi M, Szymanski C. 2008. -Linked Protein Glycosylation in , p 447-469. In Nachamkin I, Szymanski C, Blaser M (ed), , Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815554.ch25
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Image of Figure 2.
Figure 2.

Summary of biological effects caused by disruption of protein -glycosylation in .

Citation: Nothaft H, Amber S, Aebi M, Szymanski C. 2008. -Linked Protein Glycosylation in , p 447-469. In Nachamkin I, Szymanski C, Blaser M (ed), , Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815554.ch25
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Image of Figure 3.
Figure 3.

Genetic organization of gene orthologs in Proteobacteria. The commonality of the conserved gene clusters in Delta- and Epsilonproteobacteria is shown. Orthologs of Cj1119c–1132c from NCTC 11168 (NC_002163) were identified by the blastp or tblastx algorithm (http://www.ncbi.nlm.nih.gov/). The arrows indicate the transcriptional orientations of the genes; gaps between genes are indicated by either the number of open reading frames () or slashed lines indicating orthologs that were found elsewhere in the chromosome. The genes are conserved in all species examined, including subsp. 269.97 (NC-009707), RM2228 (NZ_AAFL00000000), RM2100 (NZ_AAFK00000000), RM3195 (NZ_AAFJ00000000), ATCC BAA-381 (NC_009714), 525.92 (NC_009715), 13826 (NZ_AAQZ00000000), and subsp. 82-40 (NC_008599). gene orthologs were also found in the related Epsilonproteobacteria: DSZM 1740 (NC_005090), sp. NBC37-1 (NC_009663), sp. SB55-2 (NC_009662), and in the Deltaproteobacterium G20 (NC_007519). Genes encoding the essential oligosaccharyltransferse PglB are depicted in black. Biosynthetic Pgl enzymes (Gne, PglE (E), PglF (F), PglD (D)), glycosyltransferases (PglA (A), PglJ (J), PglH (H), PglI (I), PglC (C)), and the flanking gene products PglG (G) and WlaA were designated according to their orthologs in NCTC 11168 or as glycosyltransferase if no homology to any NCTC 11168 Pgl glycosyltransferase was found. PglC orthologs in sp. NBC37-1 and sp. SB55-2 are indicated with a question mark because other proteins with a higher percentage identity (ID) to PglC of NCTC 11168 can be found in the genome of both species. Note that the PglF ortholog protein in subsp. 269.97 is annotated as a pseudogene that might be due to a sequencing error in the unfinished genome sequencing project. Orthologs to putative ABC-type transporters that show low homologies to PglK (K) of NCTC 11168 are indicated by a question mark.

Citation: Nothaft H, Amber S, Aebi M, Szymanski C. 2008. -Linked Protein Glycosylation in , p 447-469. In Nachamkin I, Szymanski C, Blaser M (ed), , Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815554.ch25
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Table 1.

Putative N-linked glycoproteins

Citation: Nothaft H, Amber S, Aebi M, Szymanski C. 2008. -Linked Protein Glycosylation in , p 447-469. In Nachamkin I, Szymanski C, Blaser M (ed), , Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815554.ch25
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Table 2.

Transcriptional profiling of mutants

Citation: Nothaft H, Amber S, Aebi M, Szymanski C. 2008. -Linked Protein Glycosylation in , p 447-469. In Nachamkin I, Szymanski C, Blaser M (ed), , Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815554.ch25
Generic image for table
Table 3.

NTCT 11168 gene orthologs

Citation: Nothaft H, Amber S, Aebi M, Szymanski C. 2008. -Linked Protein Glycosylation in , p 447-469. In Nachamkin I, Szymanski C, Blaser M (ed), , Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815554.ch25

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