Publications by authors named "David Vizarraga"
Article Synopsis
- Mycoplasma pneumoniae and Mycoplasma genitalium are bacteria that infect the human respiratory and urogenital tracts by attaching to host cells through cytoadhesins.
- These cytoadhesins bind specifically to sialylated glycans on host surfaces, making them critical for infection.
- Researchers are exploring ways to design inhibitors that block these interactions, which could lead to new treatments for infections caused by these pathogens.
Mycoplasma pneumoniae, responsible for approximately 30% of community-acquired human pneumonia, needs to extract lipids from the host environment for survival and proliferation. Here, we report a comprehensive structural and functional analysis of the previously uncharacterized protein P116 (MPN_213). Single-particle cryo-electron microscopy of P116 reveals a homodimer presenting a previously unseen fold, forming a huge hydrophobic cavity, which is fully accessible to solvent.
View Article and Find Full Text PDFMycoplasma genitalium (Mge) and Mycoplasma pneumoniae (Mpn) are two human pathogens associated with urogenital and respiratory tract infections, respectively. The recent elucidation of the tridimensional structure of their major cytoadhesins by X-ray crystallography and cryo-electron microscopy/tomography, has provided important insights regarding the mechanics of infection and evasion of immune surveillance.
View Article and Find Full Text PDFAlternative conformation of the C-domain of the P140 protein from Mycoplasma genitalium.
Acta Crystallogr F Struct Biol Commun
November 2020
The human pathogen Mycoplasma genitalium is responsible for urethritis in men, and for cervicitis and pelvic inflammatory disease in women. The adherence of M. genitalium to host target epithelial cells is mediated through an adhesion complex called Nap, which is essential for infectivity.
View Article and Find Full Text PDFArticle Synopsis
- Mycoplasma pneumoniae is a bacteria that causes atypical pneumonia, with its motility and infectivity linked to proteins P1 and P40/P90, which form an adhesion complex.
- The study determined the structures of P1 and P40/P90 using advanced techniques, revealing that the binding site for sialic acid is actually in P40/P90, not P1 as previously thought.
- Antibodies against the conserved portion of P1 showed potential in inhibiting the bacteria's adhesion, and findings suggest opportunities for developing new vaccines against M. pneumoniae infections.
Mycoplasma genitalium is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. Here we report the crystal structure of P140 both alone and in complex with the N-terminal domain of P110.
View Article and Find Full Text PDF