The citrus plant pathogen Xanthomonas citri has a dual polyamine-binding protein

Author(s)

Cremonesi, Aline Sampaio ^{[1, 2]} ; De la Torre, Lilia I. ^{[3, 2, 4]} ; de Souza, Maximillia Frazao ^[5] ; Muniz, Gabriel S. Vignoli ^[6] ; Lamy, M. Teresa ^[6] ; Oliveira, Cristiano Luis Pinto ^[5] ; Balan, Andrea ^[2]

Affiliation

^[1] Univ Sao Paulo, Programa Posgrad Interunidades Biotecnol, BR-05508900 Sao Paulo, SP - Brazil

^[2] Univ Sao Paulo, Inst Ciencias Biomed, Lab Biol Estrutural Aplicada LBEA, Dept Microbiol, BR-05508900 Sao Paulo, SP - Brazil

^[3] Univ Estadual Campinas, Programa Posgrad Genet & Biol Mol, BR-13083970 Campinas, SP - Brazil

^[4] Univ Sucre, Dept Biol & Quim, Grp Invest Biomed, Sucre 700003 - Colombia

^[5] Univ Sao Paulo, Inst Fis, Dept Fis Expt, Grp Fluidos Complexos, BR-05508090 Sao Paulo, SP - Brazil

^[6] Univ Sao Paulo, Inst Fis, Lab Biomembranas, BR-05508090 Sao Paulo, SP - Brazil

• Document type: Journal article
• Source: BIOCHEMISTRY AND BIOPHYSICS REPORTS; v. 28, DEC 2021.
• Web of Science Citations: 0

Abstract

ATP-Binding Cassette transporters (ABC transporters) are protein complexes involved in the import and export of different molecules, including ions, sugars, peptides, drugs, and others. Due to the diversity of substrates, they have large relevance in physiological processes such as virulence, pathogenesis, and antimicrobial resistance. In Xanthomonas citri subsp. citri, the phytopathogen responsible for the citrus canker disease, 20% of ABC transporters components are expressed under infection conditions, including the putative putrescine/polyamine ABC transporter, PotFGHI. Polyamines are ubiquitous molecules that mediate cell growth and proliferation and play important role in bacterial infections. In this work, we characterized the X. citri periplasmic-binding protein PotF (XAC2476) using bioinformatics, biophysical and structural methods. PotF is highly conserved in Xanthomonas sp. genus, and we showed it is part of a set of proteins related to the import and assimilation of polyamines in X. citri. The interaction of PotF with putrescine and spermidine was direct and indirectly shown through fluorescence spectroscopy analyses, and experiments of circular dichroism (CD) and small-angle X-ray scattering (SAXS), respectively. The protein showed higher affinity for spermidine than putrescine, but both ligands induced structural changes that coincided with the closing of the domains and increasing of thermal stability. (AU)

• FAPESP's process: 14/50983-3 - INCT 2014: complex fluids
• Grantee: Antonio Martins Figueiredo Neto
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 11/22386-2 - Structural caracterization and functional analysis of Nitrate/Nitrite transporter ABC type of Xanthomonas axonopodis pv. citri
• Grantee: Aline Sampaio Cremonesi
• Support Opportunities: Scholarships in Brazil - Doctorate