Abstract
The B subunit of Escherichia coli heat labile enterotoxin (LT-B) is a potent oral immunogen with potential for use as a vaccine, a carrier molecule to deliver antigens to gut-associated lymphoid tissues, and possibly an adjuvant to make coadministered vaccines more effective. LT-B produced in plants was shown to be functional and immunogenic in animals and humans. In this work, we show that maize-derived LT-B is strongly associated with starch granules in endosperm. Using immunogold labeling/electron microscopy, cell fractionation, and protein analysis techniques, we observed that LT-B protein could be detected both internally and externally in starch granules. This strong association confers an effective copurification of the antigen with the starch fraction of maize kernels, thermostability desirable in maize processing, and resistance to peptic degradation in simulated gastric fluid digests, an important attribute for an orally delivered antigen.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 11127-11132 |
| Number of pages | 6 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 100 |
| Issue number | 19 |
| DOIs | |
| State | Published - Sep 16 2003 |
Fingerprint
Keywords
- LT-B
- Starch localization
ASJC Scopus subject areas
- Genetics
- General
Cite this
Localization of a bacterial protein in starch granules of transgenic maize kernels. / Chikwamba, Rachel K.; Scott, M. Paul; Mejía, Lorena B.; Mason, Hugh; Wang, Kan.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, No. 19, 16.09.2003, p. 11127-11132.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Localization of a bacterial protein in starch granules of transgenic maize kernels
AU - Chikwamba, Rachel K.
AU - Scott, M. Paul
AU - Mejía, Lorena B.
AU - Mason, Hugh
AU - Wang, Kan
PY - 2003/9/16
Y1 - 2003/9/16
N2 - The B subunit of Escherichia coli heat labile enterotoxin (LT-B) is a potent oral immunogen with potential for use as a vaccine, a carrier molecule to deliver antigens to gut-associated lymphoid tissues, and possibly an adjuvant to make coadministered vaccines more effective. LT-B produced in plants was shown to be functional and immunogenic in animals and humans. In this work, we show that maize-derived LT-B is strongly associated with starch granules in endosperm. Using immunogold labeling/electron microscopy, cell fractionation, and protein analysis techniques, we observed that LT-B protein could be detected both internally and externally in starch granules. This strong association confers an effective copurification of the antigen with the starch fraction of maize kernels, thermostability desirable in maize processing, and resistance to peptic degradation in simulated gastric fluid digests, an important attribute for an orally delivered antigen.
AB - The B subunit of Escherichia coli heat labile enterotoxin (LT-B) is a potent oral immunogen with potential for use as a vaccine, a carrier molecule to deliver antigens to gut-associated lymphoid tissues, and possibly an adjuvant to make coadministered vaccines more effective. LT-B produced in plants was shown to be functional and immunogenic in animals and humans. In this work, we show that maize-derived LT-B is strongly associated with starch granules in endosperm. Using immunogold labeling/electron microscopy, cell fractionation, and protein analysis techniques, we observed that LT-B protein could be detected both internally and externally in starch granules. This strong association confers an effective copurification of the antigen with the starch fraction of maize kernels, thermostability desirable in maize processing, and resistance to peptic degradation in simulated gastric fluid digests, an important attribute for an orally delivered antigen.
KW - LT-B
KW - Starch localization
UR - http://www.scopus.com/inward/record.url?scp=0141479117&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0141479117&partnerID=8YFLogxK
U2 - 10.1073/pnas.1836901100
DO - 10.1073/pnas.1836901100
M3 - Article
C2 - 12960364
AN - SCOPUS:0141479117
VL - 100
SP - 11127
EP - 11132
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 19
ER -