HopA1 Effector from pv Strain 61 Affects NMD Processes and Elicits Effector-Triggered Immunity.

-secreted HopA1 effectors are important determinants in host range expansion and increased pathogenicity. Their recent acquisitions via horizontal gene transfer in several non-pathogenic Pseudomonas strains worldwide have caused alarming increase in their virulence capabilities. In , () gene confers effector-triggered immunity (ETI) against HopA1 derived from pv.

Antagonism between SUMO1/2 and SUMO3 regulates SUMO conjugate levels and fine-tunes immunity.

The attachment of SMALL UBIQUITIN-LIKE MODIFIER (SUMO) to target proteins regulates a plethora of cellular processes across eukaryotes. In Arabidopsis thaliana, mutants with abnormal SUMO1/2 conjugate levels display a dwarf stature, autoimmunity, and altered stress responses to adverse environmental conditions. Since the SUMO pathway is known to autoregulate its biochemical activity (via allosteric interactions), we assessed whether the emergence of additional SUMO paralogs in Arabidopsis has introduced the capacity of self-regulation by means of isoform diversification in this model plant.

Nuclear Localization of HopA1 Is Required for Effector-Triggered Immunity.

Plant resistance proteins recognize cognate pathogen avirulence proteins (also named effectors) to implement the innate immune responses called effector-triggered immunity. Previously, we reported that from pv. strain 61 was identified as an gene for .

Proteomic analysis of SUMO1-SUMOylome changes during defense elicitation in Arabidopsis.

Rapid adaptation of plants to developmental or physiological cues is facilitated by specific receptors that transduce the signals mostly via post-translational modification (PTM) cascades of downstream partners. Reversible covalent attachment of SMALL UBIQUITIN-LIKE MODIFIER (SUMO), a process termed as SUMOylation, influence growth, development and adaptation of plants to various stresses. Strong regulatory mechanisms maintain the steady-state SUMOylome and mutants with SUMOylation disturbances display mis-primed immunity often with growth consequences.

Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions.

The crystal structure of a 75 kDa central fragment of GBS104, a tip pilin from the 2063V/R strain of Streptococcus agalactiae (group B streptococcus; GBS), is reported. In addition, a homology model of the remaining two domains of GBS104 was built and a model of full-length GBS104 was generated by combining the homology model (the N1 and N4 domains) and the crystal structure of the 75 kDa fragment (the N2 and N3 domains). This rod-shaped GBS104 model is constructed of three IgG-like domains (the N1, N2 and N4 domains) and one vWFA-like domain (the N3 domain).

Purification, crystallization and preliminary X-ray diffraction analysis of the Staphylococcus epidermidis extracellular serine protease Esp.

Esp, an extracellular serine protease from Staphylococcus epidermidis, has been shown to inhibit S. aureus biofilm formation and nasal colonization. The full-length 27 kDa pro-Esp was purified and digested with thermolysin to obtain mature Esp.