Related Experiment Video

Updated: Feb 5, 2026

Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

10.9K

Differences in antigenic sites and other functional regions between genotype A and G mumps virus surface proteins

Sigrid Gouma1,2,3, Tessa Vermeire4,5,6, Steven Van Gucht7

  • 1Centre for Infectious Disease Control, RIVM, Bilthoven, The Netherlands.

Scientific Reports
|September 8, 2018
PubMed

Insights

Mumps virus surface proteins, fusion (F) and haemagglutinin-neuraminidase (HN), show genetic differences between pre-vaccine strains and current genotype G. These variations in B-cell epitopes and glycosylation sites on HN may explain antigenic differences and genotype G outbreaks in vaccinated populations.

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Mumps virus surface proteins, fusion (F) and haemagglutinin-neuraminidase (HN), are critical for pathogenesis and immune targeting.
  • Genotype G mumps virus is prevalent in recent outbreaks, particularly in vaccinated communities in Western Europe, the USA, and Japan.
  • The Jeryl Lynn vaccine strain belongs to genotype A.

Purpose of the Study:

  • To compare the amino acid sequences of F and HN genes from pre-vaccine era Dutch mumps virus strains with genotype G strains.
  • To investigate potential antigenic differences and their contribution to genotype G outbreaks in vaccinated populations.

Main Methods:

  • Comparative analysis of predicted amino acid sequences of mumps virus F and HN genes.
  • Focus on Dutch mumps virus samples from the pre-vaccine era (1957-1982) and genotype G strains (post-2004).
  • Identification of differences in B-cell epitopes and N-linked glycosylation sites on the HN protein.

Main Results:

  • Significant amino acid differences were identified between genotype A (Jeryl Lynn vaccine) and genotype G strains.
  • Eight variable amino acid positions were found in five known B-cell epitopes of the HN protein, specific to either genotype A or G.
  • Differences were also observed in and near sites on the HN protein associated with mumps virus pathogenesis.

Conclusions:

  • Amino acid variations in HN protein epitopes and glycosylation sites likely contribute to antigenic differences between Jeryl Lynn vaccine and genotype G strains.
  • Observed genetic differences in HN may play a role in the emergence and persistence of genotype G mumps virus outbreaks in vaccinated communities.

More Related Videos

Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods09:12

Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods

Published on: May 11, 2018

7.3K
Extraction of Tissue Antigens for Functional Assays08:32

Extraction of Tissue Antigens for Functional Assays

Published on: September 10, 2012

11.3K

Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.1K
What are Viruses?00:50

What are Viruses?

Overview
128.3K
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
30.0K
Structural Protein Function01:56

Structural Protein Function

3.3K
Mechanical Protein Functions01:58

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
5.6K