The surface genome of the Hepatitis B virus (HBV) houses three gene segments, namely PreS1, PreS2, and S. These fragments, expressed by their corresponding genes, conjoin at varying lengths to form three distinct sizes of surface proteins - small (S), medium (M), and large (L). The S protein, developed solely from the S gene, is the most abundant hydrophobic polypeptide. The M protein augments this by adding polypeptide chains encoded by the PreS2 region. The L protein, on the other hand, incorporates an amino acid end from the PreS1 region, building upon the M protein.
Scientific research has validated that the S and L proteins are essential viral proteins for the generation of intact viral particles, while the inhibition of the M protein does not impact viral morphology. Although empirical data are somewhat scarce, these surface proteins turn out to play a pivotal role in the process of HBV virus-host invasion. They house multiple antigenic epitopes, thereby positioning them as reliable and potential diagnostic markers for HBV infection, indeed conduits for intervention strategies.
Fig.1 Structure of HBV surface antigen.1
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