Unlock instant, AI-driven research and patent intelligence for your innovation.

Fusion protein and transgenic plant expressing said protein

a technology of fusion protein and transgenic plant, which is applied in the field of nuclear acid molecules, can solve problems such as inability to produ

Active Publication Date: 2019-08-20
UNIV DEGLI STUDI DI ROMA LA SAPIENZA
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0012]The authors have demonstrated that Arabidopsis plants expressing a chimeric protein obtained from the fusion between a fungal PG and a PGIP accumulate OGs in plant tissues and hence activate the plant defense responses. Furthermore, plants expressing this fusion protein (called OG-machine, initials OGM), under the control of a pathogen-inducible promoter, have an increased resistance against pathogenic microorganisms such as fungi and bacteria. The present data demonstrate that it is possible to engineer the release of DAMPs so as to be able to induce plant immunity in vivo. OGMs and DAMPs are thus powerful tools capable of providing protection to the plant against pathogens.

Problems solved by technology

Further, plants simultaneously expressing the PGII of Aspergillus niger and the PGIP2 of Phaseolus vulgaris, which is able to inhibit the PGII of A. niger, obtained by crossing two transgenic plants separately expressing either PG or PGIP, do not allow the production of OG in vivo (Ferrari S, Galletti R, Pontiggia D, Manfredini C, Lionetti V, Bellincampi D, Cervone F, De Lorenzo G: Transgenic expression of a fungal endo-polygalacturonase increases plant resistance to pathogens and reduces auxin sensitivity.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Fusion protein and transgenic plant expressing said protein
  • Fusion protein and transgenic plant expressing said protein
  • Fusion protein and transgenic plant expressing said protein

Examples

Experimental program
Comparison scheme
Effect test

example

Materials and Methods

Strains

[0108]E. coli DH5α [genotype: F-φ80lacZΔM15 Δ(lacZYA-argF)U169 deoR recA1 endA1 hsdR17(rk, mk+) phoA supE44 thi-1 gyrA96 relA1 λ-(Invitrogen)

[0109]A. tumefaciens LBA4404 (INVITROGEN, catalogue number: 18313-015)

[0110]P. pastoris X33 (wild type) (Invitrogen)

[0111]A. thaliana Col-0 (wild type) (purchased from Lehle Seeds)

Construction of the Gene Cassette for the Expression of the Chimeric Fusion Protein PG-PGIP (OGM) in P. pastoris (Corresponding to the Amino Acid Sequence of the OGM Expressed in Pichia (SEQ ID NO:8))

[0112]For the expression of the fusion protein in P. pastoris, the 5′ end of the gene coding for PvPGIP2 was fused to the sequence coding for the alpha factor of yeast present in the integrative vector pGAPZ alpha which enables the constitutive expression of the transgene; the construct pGAPZα-PGIP2 was thus obtained. The gene coding for the mature protein PvPGIP2 was amplified by means of specific primers (EcoRIPGIP2Fw (SEQ ID NO: 10) and NotI...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
timeaaaaaaaaaa
pHaaaaaaaaaa
volumeaaaaaaaaaa
Login to View More

Abstract

The present invention concerns a nucleic acid molecule capable of expressing, in at least one plant tissue, a chimeric protein comprising a polygalacturonase (PG) of fungal, bacterial or insect origin and a plant polygalacturonase inhibitor protein (PGIP) plant capable of inhibiting said PG. The present invention also relates to transgenic plants that express said chimeric protein.

Description

RELATED CASES[0001]This application is the national stage entry under 35 U.S.C. § 371 of International Patent Application No. PCT / EP2015 / 081017, filed on Dec. 22, 2015, which claims the benefit of Italian Patent Application No. RM2014A000748, filed on Dec. 23, 2014, the entirety of each of which is incorporated herein by reference.TECHNICAL FIELD[0002]The present invention concerns a nucleic acid molecule capable of expressing, in at least one plant tissue, a chimeric protein comprising a polygalacturonase (PG) of fungal, bacterial or insect origin and a plant polygalacturonase inhibitor protein (PGIP) capable of inhibiting said PG. The present invention also relates to transgenic plants that express said chimeric protein.PRIOR ART[0003]Plant immunity is mediated not only by pathogen-derived molecules, called microbe-associated molecular patterns (MAMPs) (1), but also by endogenous molecules referred to as damage-associated molecular patterns (DAMPs), which are released by the host ...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Patents(United States)
IPC IPC(8): C12N15/62A01N25/10C07K14/195C07K14/435C07K14/415C12N15/82C07K14/37
CPCC12N15/62A01N25/10C07K14/195C07K14/37C12N15/8286C07K14/43563C12N15/8279C12N15/8281C12N15/8282C07K14/415
Inventor CERVONE, FELICEDE LORENZO, GIULIAFERRARI, SIMONEBENEDETTI, MANUELPONTIGGIA, DANIELA
Owner UNIV DEGLI STUDI DI ROMA LA SAPIENZA