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Varki A, Cummings RD, Esko JD, et al., editors. Essentials of Glycobiology. 2nd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009.

Cover of Essentials of Glycobiology

Essentials of Glycobiology. 2nd edition.

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This page maintains a record of all major corrections that have been made to the online version of Essentials of Glycobiology, 2nd Edition. The corrections identified on this page had not been made to the print copy at the time of its first printing in October, 2008.

These corrections are maintained and edited by the book’s principal editors. They are organized by the date on which they were made, the most recent corrections being listed first.

August 2011

Change to Figure 39.5

The major gp120 receptor is CD4 and CXCR4, not CCR4 as indicated in the original figure.

January 2011

Change to Figure 1.6

(i) The original figure depicts a PO4 group located on a penultimate mannose residue in the N-linked glycan. Although early studies of lysosomal enzymes showed a phosphate group on a penultimate mannose residue, the terminal mannose residue is eventually removed to reveal a PO4 group at C-6, generating the mannose-6-PO4 recognition determinant. (ii) The chain indicated as chondroitin sulfate contained an iduronic acid residue, which is characteristic of dermatan sulfate. The iduronic acid units were removed and a new dermatan sulfate chain was added to the idealized proteoglycan.

Change to text in Chapter 4

In the section “General Principles,” Reaction 3 has been edited.

Change to Figure 4.1

(i) The asterisk indicating regulated steps in nucleotide sugar formation was incorrectly positioned at the glucosamine-6-PO4 acetyltransferase and should be located at the fructose-6-PO4 amidotransferase. (ii) N-acetylneuraminic-6-PO4 should be N-acetylneuraminic-9-PO4. (iii) ManNAc can be converted to Neu5Ac via Sialate:pyruvate lyase action as shown in the lower part of the figure. Readers should be aware that ManNAc can also be interconverted with GlcNAc under some conditions.

Change to text in Chapter 9

In the section “Synthesis of O-GalNAc Glycan Core Structures,” the following text was edited to read: “Cosmc is an ER protein that appears to bind specifically to T synthase and ensures its full activity in the Golgi. Lack of core 1 synthesis can be due to either defective T synthase or the absence of functional Cosmc chaperone. The result is high expression of Tn and sialyl-Tn antigens.”

In the section “Functions of O-GalNAc Glycans,” the following text was edited to read: “Some sugar residues or their modifications can mask underlying antigens or receptors. For example, O-acetyl groups on the sialic acid residue of the sialyl-Tn antigen prevent recognition by anti-sialyl-Tn antibodies. Gut bacteria enzymatically remove this blocking group.”

Change to Figure 9.3

Cosmc, the T-synthase chaperone, was inadvertently omitted from the figure.

Change to text in Chapter 11

In the section “Membrane Properties of GPI-Anchored Proteins,” “Toll-like receptor-2” was changed to “Toll-like receptor-4.” The sentence now reads: “Similarly, GPI-anchored CD14 (the LPS/LPS-binding protein receptor) functions equally well with a GPI anchor or with a spliced transmembrane domain, and the signal-transducing partner for CD14 has been identified as the transmembrane Toll-like receptor-4.”

Change to text in Chapter 13

In the section “Poly-N-acetyllactosamines,” the following sentence was deleted: “Glycoproteins and glycolipids frequently bear N-glycans, O-glycans, and glycolipids with poly-N-acetyllactosamine chains.”

Change to Table 16.3

The text was corrected to designate syndecans having 1-3 HS and 1-2 CS, not 1-3 CS and 1-2. Formatting in the Tissue Distribution column was altered to show the appropriate tissue distribution for Syndecans 1–4 and Betaglycan.

Changes to text in Chapter 20

In the Summary section, the text now reads: “Bacterial glycans include peptidoglycan, periplasmic glucans, lipopolysaccharide, glycans of surface layer (S layer) proteins, and extracellular polysaccharides that make up capsules and biofilms. In Archaea, the cell surface consists of an S layer, which is mainly composed of glycosylated S layer proteins and, in methanogens, also of pseudomurein.”

In the Background section, the text now reads: “They lack the peptidoglycan found in almost all prokaryotes and instead, in methanogens, contain a pseudomurein layer, which is similar to the peptidoglycan structure. In general, archaeal structures have been studied in less detail than the corresponding bacterial structures.”

Change to Table 20.1

“Group B Streptococcus” was changed to “Group A Streptococcus.”

Change to text in Chapter 30

In the section “Enzymatic Mechanism for Generation of the M6P Recognition Marker,” “Uridine-P+GlcNAcα1-6-Manα1-(N-glycan)-Lysosomal enzyme” was changed to “Uridine-P+GlcNAcα1-P-6-Manα1-(N-glycan)-Lysosomal enzyme” in the second reaction of the biochemical pathway graphic.

Change to Figure 36.2

Current evidence suggests that the N-linked glycan on misfolded glycoproteins destined for export from the ER and destruction are trimmed from nine mannose residues to seven.

Change to text in Chapter 50

In the section “Sulfotransferase Inhibitors,” “PAPS” was changed to “PAP” in the following sentence: “For example, β-arylsulfotransferase IV (β-AST-IV) will catalyze the reverse transfer of the sulfuryl group from p-nitrophenol sulfate to PAP, generating PAPS and p–nitrophenolate ion.”

Changes to the Glossary

In the entry for Heparan sulfate, “(GlcNAcα1–4GlcAβ1–4IdoAα1–4) n” was changed to “(GlcNAcα1–4GlcAβ1–4/IdoAα1–4) n”.

In the entry for Complex glycan, “then” was changed to “than.” The entry now reads: “A glycan containing more than one type of monosaccharide.”

March 2010

Change to Figure 11.2

The sugar residues attached to the N-acetylgalactosamine unit in the GPI anchor of Toxoplasma SAG-1 (Fig. 11.2B) and to the terminal mannose unit in Torpedo AChE (Fig. 11.2C) should be glucose, not fucose as indicated.

December 2009

Change to text in Chapter 27

In the Historical Background section, “Corey” was changed to “Florey.”

October 2009

Change to Figure 13.19

The sugar residues attached to the N-acetylglucosamine units in the antennae should be galactose, not N-acetylgalactosamine as indicated.

August 2009

Change to Figure 1.5

The following RGB settings were added: “*Note: To reproduce precise colors in RGB format, use the following triplet values: Galactose stereochemistry: Yellow (255,255,0); Glucose stereochemistry: BLUE (0,0,250); Mannose stereochemistry: GREEN (0,200,50); Fucose: RED (250,0,0); Xylose: ORANGE (250,100,0); Neu5Ac: PURPLE (125,0,125); Neu5Gc: LIGHT BLUE (200,250,250); KDN: GREEN (0,200,50); GlcA: BLUE (0,0,250); IdoA: TAN (150,100,50); GalA: Yellow (255,255,0); ManA: GREEN (0,200,50).”

January 2009

Change to Figure 8.1

The original drawing depicted a hybrid chain containing two outer α2-linked mannose residues, which is not known to occur in nature. The correct structure contains only five mannose residues.

December 2008

Change to Figure 2.1b

The left and right images in Figure 2.1b have been transposed. The labels have not been changed.

Corrected title for Teaching Slide 1.2

In the title of Teaching Slide 1.2, the term “galactose” has been changed to “glucose.” The title now reads “Open-chain and ring forms of glucose”.

Modified References in Chapter 14

The References section of Chapter 14 has been modified. Schauer, R. and Kamerling, J.P. 1998 was removed and replaced by the following two references:

Schauer R and Kamerling JP 1997. Chemistry, biochemistry and biology of sialic acids. In: Glycoproteins II (Montreuil J, Vliegenthart JFG and Schachter H, eds.), pp. 243-402, Elsevier, Amsterdam.

Traving C and Schauer R 1998. Structure, function and metabolism of sialic acids. CMLS, Cell Mol Life Sci 54:1330-1349.

“Polylactosamine” changed to “poly-N-acetyllactosamine”

In Chapters 8, 42, 46, and 47, and in the glossary, the term “polylactosamine” has been changed to “poly-N-acetyllactosamine”.

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Copyright © 2009, The Consortium of Glycobiology Editors, La Jolla, California.
Bookshelf ID: NBK3820


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