Background:
The immune system is able to recognize substances that originate from inside
or outside the body and are potentially harmful. Foreign substances that bind to immune system
components exhibit antigenicity and are defined as antigens. The antigens exhibiting immunogenicity
can induce innate or adaptive immune responses and give rise to humoral or cell-mediated
immunity. The antigens exhibiting mitogenicity can cross-link cell membrane receptors on B and T
lymphocytes leading to cell proliferation. All antigens vary greatly in physicochemical features
such as biochemical nature, structural complexity, molecular size, foreignness, solubility, and so
on.
Objective::
Thus, this review aims to describe the molecular bases of protein-antigenicity and those
molecular bases that lead to an immune response, lymphocyte proliferation, or unresponsiveness.
Conclusion:
The epitopes of an antigen are located in surface areas; they are about 880-3,300 Da
in size. They are protein, carbohydrate, or lipid in nature. Soluble antigens are smaller than 1 nm
and are endocytosed less efficiently than particulate antigens. The more the structural complexity
of an antigen increases, the more the antigenicity increases due to the number and variety of epitopes.
The smallest immunogens are about 4,000-10,000 Da in size. The more phylogenetically distant
immunogens are from the immunogen-recipient, the more immunogenicity increases. Antigens
that are immunogens can trigger an innate or adaptive immune response. The innate response is induced
by antigens that are pathogen-associated molecular patterns. Exogenous antigens, T Dependent
or T Independent, induce humoral immunogenicity. TD protein-antigens require two epitopes,
one sequential and one conformational to induce antibodies, whereas, TI non-protein-antigens require
only one conformational epitope to induce low-affinity antibodies. Endogenous protein antigens
require only one sequential epitope to induce cell-mediated immunogenicity.