There are many immunology textbooks that have chapters on this. I would recommend textbooks or review articles over the primary research papers because there are thousands of research papers on this and you should start with a good introductory summary of what is known.

Thanks for sharing your idea Brian. But textbooks are always describe the classical process of antigen presentation in which the antigen are digested. I am thinking about how the immune cell present the epitope which has intact 3D structure.

Dear Linhui Wang,

Our immune system does not possess the capability to present a peptide or an epitope with intact 3D structure. However, B cell epitopes (conformational may be linear or non-linear) often plays the recognition of 3D structure of a specific epitope. In general, complement proteins can recognize the conserved three dimensional part of a protein. Of note, we won't use the word "present" but we use the word "recognition". The primary reason "present" - undergoes APP machinery whereas recognition is intact identification of 3D structure. In simpler words, complement system is the answer for your question. The complement system mediated B cell memory also plays a vital role in memorizing a specific 3D pattern (in your terms - intact epitope).

@ Narayanan Kalyanaraman

Dear Dr. Kalyanaraman,

Thank you so much for your great answer. I have got a lot of information from your answer, but I could only understand few of them. So, do you have any paper describe "The complement system mediated B cell memory also plays a vital role in memorizing a specific 3D pattern"?

Thanks again.

Dear Linhui Wang,

Unfortunately, we cannot find a single paper to understand this concept. It's a collective knowledge on different concept. Please read about the role of complement system in regulation of B cell memory, B cell tolerance or humoral immunity. I would like to give an orientation: B Cell Memorize conformational epitope - Complement system regulates B cell memory. From this we can easily conclude that memory of a 3D pattern stems from B cell rather than complement proteins. Hence, please find papers or reviews that deal with B cell conformational non-linear epitopes and its way of memory.... It will answers or explains bettern than me

Narayanan Kalyanaraman

Hi Narayanan Kalyanaraman,

I have got these two articles, please check them. I think the repetitive epitopes on VLPs pretty much like the repetitive epitopes polysachrides, in terms of cross-linking the BCRs.

1.T-cell-independent antiviral antibody responses

Eva Szomolanyi-Tsuda and Raymond M Welsh

2. T cell-independent B cell memory

Thierry Defrance, Morgan Taillardet and Laurent Genestier

Hi Linhui wang,

Do you have full text of these papers? i don't have access for these materials. I will read and give my opinions at the earliest

Narayanan Kalyanaraman

Hi Dr. Kalyanaraman,

Please check your in-mail of your message.

Linhui.

Hi Linhui Wang,

Thanks for message. Yes, you are right - the repetitive epitopes on VLPs pretty much like the repetitive epitopes polysachrides.

The mechanism behind the hypothesis of the antiviral T1 antibody response reported are often related with viral antigens repetitively displayed in the virions is not clear by that time (around 1998). Hence, we cannot conclude that B cell recognize such repetitive antigenic arrays directly as a cognate.

However, now we know that B cell can function as professional APC. Hence, logically we can conclude that the appearance of strong B cell response for certain antigenic epitopes (without the support of T cell machinery) can originate from B cell presented linear (conformational) epitopes. Thus, such epitope cannot be discontinuous conformational epitopes.

The second review clearly suggested the influence of B cell receptor (BCR) ( for recognition of antigen without presentation). Hence, the antigenic repetitive array must form a conformation but it can be derived from a discontinuous or linear peptides. Theoretically, repetition of peptides (arrays) has to be linear and forms a definite conformation to cross link BCR.