4  Case Study: Rituximab

In this week’s lecture, prof. Asial runs through some common tips for searching for information on the web. He also illustrates his findings (as an example) on the FDA-approved antibody Rituximab.

Optional Reading for Class

Prof. Asial also recommends the above reading for those who want to know more about therapeutic antibodies and their use in diseases.

4.1 Potential Sources and Trail Following

Prof. Asial lists some sources:

  1. Nature Reviews

    Nature Reviews’ Search Engine

    Nature Reviews provides rigorous review articles on scientific topics.

  2. Google Images

    Using Google Images to Search for Mechanisms of Action

    Google Images is a nice starting place when trying to look for graphics to explain an antibody’s mode of action.

  3. PubMed

    PubMed’s Search Engine

    PubMed is also a nice starting point to search for information.

  4. Google Scholar

    Google Scholar’s Search Engine

    This is a very common search engine used to search for scholarly information, yet is also a good starting point.

4.1.1 Reading Articles

References in Articles

Often times in papers, author(s) may reference one or more papers. In some cases, following the reference trail may be handy in helping to find information about the antibody.

Antibodies may also have different names - as is the case with Rituximab.

4.2 Case Study on Rituximab

Lymphoma is a cancer of the lymphocytes (i.e., B and / or T-cells).

A Stained Reed-Sternberg Cell on Display

In Hodgkin lymphoma patients, patients exhibit Reed-Sternberg cells (i.e., giant lymphocytes).

Lymphoma cases represent 2.8% of all cancer cases (about 510000 cases) worldwide and 2.6% of all cancer-related fatalities (about 250000 deaths) worldwide.

In Singapore, lymphoma represents 4.7% of all cancer cases (about 1099 cases) and about 3% of all cancer-related fatalities (about 361 deaths). It is also the 5th most common cancer among males.

4.2.1 Possible Mechanisms and Treatment

Illustration of B Cell Maturation

When B-cells mature, they begin expressing a protein called Cluster of Differentiation 20 (i.e., CD20). Newly-formed B-cells do not express this protein.

Hence, a potential therapy for Hodgkin lymphoma could be to deplete B-cell numbers via targeting with monoclonal antibodies.

4.2.2 Rituximab’s Mode of Action

Rituximab’s Mode of Action

When Rituximab binds to a B-cell (i.e., opsonization), the tagged B-cell can be eliminated on one of three ways:

  1. Complement Activation Cascade

    This was covered during week 2. The cascade eventually results in the recruitment of protein called the membrane attachment complex (i.e., MAC). This protein causes lysis and elimination via antibody-dependent cellular cytotoxicity (i.e., ADCC).

  2. Antibody-Dependent Cellular Phagocytosis (i.e., ADCP)

    The crystallizable fragments of Rituximab can also recruit macrophages to the site of infection for phagocytosis.

  3. NK Cell Recruitment

    The antibody can also recruit NK cells to the site of infection via Fc\(\gamma\)RIII receptors.

4.2.3 CD20 Target

Schematic of the CD20 Protein

CD20 is an integral protein that is exclusively expressed by B-cells. It has four trans-membrane alpha helices and two extracellular loops (where Rituximab binds).

CD20 is thought to be involved in B-cell differentiation, if not also function as an ion channel (though this yet to be confirmed).

Structure of CD20

Via cryo-electron microscopy, it is confirmed that CD20 is a dimer tha binds two Rituximab antigen binding fragments (Rituximab mainly binds to the ECL2 region of CD20).

4.2.4 Antibody Discovery, Expression, and Purification

Binding Affinity Graphs of Rituximab

Rituximab is identified by hybridoma cells and cloned into mammalian expression vectors. The antibody is expressed in CHO cells and purified via protein A chromatography.

In another source, the authors claim that the antigen-binding fragments of Rituximab can also be produced in bacterial perplasm; antibodies (i.e., the IgG variety) are produced in HEK293 cells before they are secreted into extracellular media. The authors used protein G chromatography and size-exclusion chromatography.