Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans

There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

Abstract

A functional comparison was made between a monoclonal secretory antibody generated in transgenic plants and its parent murine IgG antibody.The affinity constants of both antibodies for a Streptococcus mutans adhesion protein were similar. However the secretory antibody had a higher functional affinity due to its dimeric structure. In the human oral cavity, the secretory antibody survived for up to three days, compared with one day for the IgG antibody. The plant secretory antibody afforded specific protection in humans against oral streptococcal colonization for at least four months. We demonstrate that transgenic plants can be used to produce high affinity, monoclonal secretory antibodies that can prevent specific microbial colonization in humans. These findings could be extended to the immunotherapeutic prevention of other mucosal infections in humans and animals.

Related collections

Most cited references 8

Record: found
Abstract: found
Article: not found

A three-tiered view of the role of IgA in mucosal defense.

M B Mazanec, J G Nedrud, C S Kaetzel … (1993)

Mucosal IgA has generally been viewed as an immune barrier to prevent the adherence and absorption of antigens. Recent studies employing polarized epithelial monolayers have suggested two additional functions for mucosal IgA. One is to neutralize intracellular microbial pathogens, such as viruses, directly within epithelial cells. The second is to bind antigens in the mucosal lamina propria and excrete them through the adjacent epithelium into the lumen, thereby ridding the body of locally formed immune complexes and decreasing their access to the systemic circulation.

0 comments Cited 56 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: not found
Book Chapter: not found

Immunoglobulin A (IgA): Molecular and Cellular Interactions Involved in IgA Biosynthesis and Immune Response

Jiri Mestecky, Jerry McGhee (1987)

0 comments Cited 44 times – based on 0 reviews

Bookmark

Record: found
Abstract: found
Article: not found

Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants.

P Stabila, C Fux, T Lehner … (1993)

The genes encoding the heavy and light chains of a murine monoclonal antibody (mAb Guy's 13) have been cloned and expressed in Nicotiana tabacum. Transgenic plants have been regenerated that secrete full-length Guy's 13 antibody. By manipulation of the heavy chain gene sequence, constant region domains from an immunoglobulin alpha heavy chain have been introduced, and plants secreting Guy's 13 mAb with chimeric gamma/alpha heavy chains have also been produced. For each plant antibody, light and heavy chains have been detected by Western blot analysis and the fidelity of assembly confirmed by demonstrating that the antibody is fully functional, by antigen binding studies. Furthermore, the plant antibodies retained the ability to aggregate streptococci, which confirms that the bivalent antigen-binding capacity of the full length antibodies is intact. The results demonstrate that IgA as well as IgG class antibodies can be assembled correctly in tobacco plants and suggest that transgenic plants may be suitable for high-level expression of more complex genetically engineered immunoglobulin molecules. Since mAb Guy's 13 prevents streptococcal colonization in humans, transgenic plant technology may have therapeutic applications.