AN

ASSIGNMENT REPORT
ON
O-LINKED GLYCOPROTEINS

STUDENT’S NAME: HARISH K

SRN No.: R19MBT69

Semester: 1
Year/Batch: JULY 2019_ TO DEC., 2021_
Department: BIOTECHNOLOGY

Mobile No: 9751568224

Email id: harishkrishnan100@gmail.com
FACULTY IN-CHARGE: Dr.RAMACHANDRAN

MY SIGN.jfif
Assignment Report No: 1

_________________
Name and Signature of Student
INTRODUCTION

After post translation, proteins can be further modified by being

attached to carbohydrate groups (sugars) by glycosidic bonds via
the process called glycosylation, and the newly formed molecule
is called a glycoprotein. There are two types of glycosidic bonds
that can occur in this process, called N-linkage and
O-linkage. N-linkage: The nitrogen atom in the side chain of
Asparagine is attached to the sugar. The sequence can be
Asn-X-Ser or Asn-X-Thr, where X is any kind of amino acid
except proline. O-linkage: The oxygen atom in the side chain of
serine or threonine amino acids is attached to the sugar.O-Linked
glycoproteins are usually large proteins with a molecular mass
of >200 kDa. Glycosylation generally occurs in high-density
clusters and may represent as much as 50-80% of the overall
mass.
STRUCTURE
O-Linked glycans are most commonly attached to the peptide
chain through serine or threonine residues. While O-linkage
does link primarily to peptide residues through a hydroxyl
group, there is no consensus sequence required. Tyrosine,
hydroxylysine , or hydroxyproline may also be the peptide site
of O-linked glycosylation. The most common O-linked glycans
are the mucin- type glycans, which contain an initial GalNAc
residue. Even with common mucin-type cores, O-linked glycans
tend to be very heterogeneous, and there are other structures
possible, in addition to several sialylated core structures.
However, O-linked glycans are commonly linear or biantennary
and have comparatively less branching than N-glycans.

There are eight mucin- type core structures;

BIOSYNTHESIS
This process is the step-wise addition of the sugar residues
directly onto the polypeptide chain. It occurs in the Golgi.

 At first the N-Acetylgalactosamine residue is transferred

from UDP-GalNAc to the hydroxyl group of Ser or Thr
residue. It is catalyzed
by N-Acetylgalactosaminyltransferase.
UDP-GalNAc is synthesized from UDP-glucose.
 Then the protein moves to the trans-Golgi vesicles where the
carbohydrate chain is elongated. The specific
glycosyltransferase adds the galactose residue to the
GalNAc.
 The last steps in biosynthesis of typical O-glycans are the
additions of two N-Acetylneuramic acid (sialic acid) residues
in the trans-Golgi reticulum.
MUCIN
Mucins are glycoproteins that contain large numbers of
high-density clusters of O-linked glycans. The mucin-type
glycans of these proteins frequently form cross-linked
connections in aqueous solutions, resulting in a high viscosity
gel (mucus). Mucins can be secreted, but may also be membrane
bound and form glycan-dense areas on the cell surface. In
addition to mucin-type glycans, O-linked glycans may
incorporate sugars other than GalNAc as the initial sugar bound
to the serine/ threonine residues. Mucins are negatively charged,
which allows them to interact with water and prevent it from
evaporating. This is important in their protective function as it
lubricates the tracts so bacteria cannot bind and infect the body.
Changes in mucins are important in numerous diseases,
including cancer and inflammatory bowel disease. Absence
of O-glycans on mucin proteins changes their 3D shape
dramatically and often prevents correct function.
 Examples of alternative O-linked glycans are:
 Nuclear and cytoplasmic glycoproteins that contain GlcNAc
as the initiating sugar.
 Fibrinolytic and coagulation factors that contain fucose as
the initiating sugar.
 Mannoproteins that are typical to yeasts and that incorporate
mannose as the initiating sugar.
 O-Mannosyl glycans are also found in human
α-dystroglycan and other nervous system glycoproteins.
 Glycosaminoglycans (GAGs) that are components of
proteoglycan structures and contain xylose bound
exclusively to serine residues.
 Plant cell wall extensins that contain both arabinose attached
to hydroxyproline and galactose attached to serine.
 Plant arabinogalactans that are attached to the
hydroxyproline within the peptide backbone through
O-linked galactose or glucose.
 Galactose and αGlc(1→2)Gal residues that are bound to
hydroxylysine within the triple helix structures of collagen.
Complement factor C1q also contains
αGlc(1→2)Gal-hydroxyproline sequences. • Glycogenin, a
protein precursor required for glycogen synthesis, contains
glucose O-linked to tyrosine; the initial glucose is
subsequently elongated by glycogen synthase to generate
glycogen.

FUNCTIONS
 O-GalNAc sugars are important in a variety of processes,
including leukocyte circulation during an immune response,
fertilisation, and protection against invading microbes
 O-GalNAc sugars are common on membrane glycoproteins,
where they help increase rigidity of the region close to the
membrane so that the protein extends away from the surface.
 In order for leukocytes of the immune system to move into
infected cells, they have to interact with these cells
through receptors.
 Leukocytes express ligands on their cell surface to allow
this interaction to occur. P-selectin glycoprotein ligand-1
(PSGL-1) is such a ligand, and contains a lot of O-glycans
that are necessary for its function.
 O-glycans near the membrane maintain the elongated
structure and a terminal epitope is necessary for interactions
with the receptor.
 Mucins are a group of heavily O-glycosylated proteins that
line the gastrointestinal and respiratory tracts to protect these
regions from infection.

CONCLUSION
O-linked glycoprotiens are those The oxygen atom in the side
chain of serine or threonine amino acids is attached to the sugar.
These o-linked glycoprotiens are formed in the golgi bodies and
then they will be converted into granules or lysosomes. There
are many O-linked glycoproteins which helps in different
functions of the body. These biological molecule can plays a
variety of roles and can be found in the extra cellular matrix.
REFERENCE

 https://www.sigmaaldrich.com › biology › glycobiology-pdf ›

o-glycans

 https://link.springer.com/article/10.1007%2FBF01049675

 Engelking, L. R. (2015). Glycoproteins and Glycolipids.

Textbook of Veterinary Physiological Chemistry, 130–
135. doi:10.1016/b978-0-12-391909-0.50020-7