Brucella abortus MFP: a trimeric coiled-coil protein with membrane fusogenic activity.
The bacterial genus Brucella consists of a group of facultative intracellular pathogens which produces abortion and infertility in animals and a chronic debilitating febrile illness in humans. BMFP is a basic protein of Brucella abortus that belongs to a highly conserved group of homologue proteins of unknown structure and function in proteobacteria (COG2960). In this study, we report the structural and biochemical characterization of this protein. We found that BMFP has two structural domains: a carboxyl-terminal coiled-coil domain through which the protein self-associates as a trimer and a natively disordered amino-terminal domain which has propensity to adopt an amphipathic alpha-helical structure. This natively unfolded domain undergoes a structural rearrangement from unfolded to alpha-helix in the presence of high ionic strength, acidic pH, detergents, and phospholipid vesicles. Moreover, we demonstrated that the interaction of BMFP with phospholipid vesicles promotes in vitro membrane fusion. These results contribute to the elucidation of the structural and functional properties of this protein and its homologues present in most proteobacteria.
Carrica
Mariela del Carmen
Mdel C
Instituto de Biotecnología, CICVyA, INTA, Los reseros y las cabanas s/n, Castelar, Buenos Aires, Agentina. carricamariela@yahoo.com.ar
Craig
Patricio Oliver
PO
Alonso
Silvia del Valle
Sdel V
Goldbaum
Fernando Alberto
FA
Cravero
Silvio Lorenzo
SL
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002003:Brucella abortus / Q000235:genetics / Q000378:metabolism*; D002942:Circular Dichroism; D019281:Dimerization; D008081:Liposomes / Q000737:chemistry; D008561:Membrane Fusion; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010743:Phospholipids / Q000737:chemistry / Q000378:metabolism*; D016133:Polymerase Chain Reaction; D011485:Protein Binding; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013050:Spectrometry, Fluorescence
D001426:Bacterial Proteins; D008081:Liposomes; D008563:Membrane Lipids; D010743:Phospholipids