Glycosylation Sites

For glycosylation sites analysis, analysis of N-linked, O-linked, and C-linked glycosylation sites was done for all the HPV strains found on NCBI website.

N Linked Sites
O Linked Sites
C Linked Sites

N-glycosylation is a type of post translational modification that plays a crucial role in viruses such as proteolytic process, protein trafficking, receptor binding, virus assembly, virulence, immune evasion, etc.

The most common N-linked glycosylation sites found in proteins are as follows:

> El : 31,53,272,314

> E2 : 21,83,84,133,134,219,252

> E6 : 80

> E7 : 5,29,71

> L1 : 216

> L2 : 143,149,159,160,208,209,394,397,419

E1
E2
E4
E5
E6
E7
L1
L2
Major Capsid
Minor Capsid
Regulatory
Replication
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In O-linked glycosylation sites, they have a function in various biological activities such as signal transduction, ligand recognition, virus/bacteria-host interactions etc.

The most common O-linked glycosylation sites in proteins are as follows:

> El : 168,167,166

> E2 : 207,247,264

> E4 : 47

> E6 : 6

> L2 : 133,134,156,212,213

E1
E2
E4
E6
E7
L1
L2
Major Capsid
Minor Capsid
Regulatory
Replication
Transforming
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The function of the C-linked glycosylation sites is unknown, they may play a role in enzymatic activity and secretion. C-linked glycosylated sites in proteins are significant, but were unable to identify any potential glycosylation sites (any site cannot reach 0.5 threshold of the software).