Fig. 1
From: Role of Verticillium dahliae effectors in interaction with cotton plants

V. dahliae uses its many types of effectors to manipulate host immunity. VdAl protects transcription factor MYB6 from degradation by interacting with the E3 ligases PUB25 and PUB26 to enhance Verticillium wilt resistance. VdIsc1 disrupts the plant salicylate metabolism pathway by suppressing the transformation from isochorismate to salicylic acid. VdEix3 exhibits immunity inducing activity in Nicotiana benthamiana, recognized by the leucine-rich repeat receptor-like protein NbEix2. VdNlp1 and VdNlp2 are glycosylinositol phosphorylceramide (GIPC) sphingolipids that act as necrosis- and ethylene-inducing-like protein (NLP) toxin receptors; NLPs form complexes with terminal monomeric hexose moieties of GIPCs and insert into the plant plasma membrane, causing cell lysis. VdXyn4 plays a cytotoxic function and induces a necrosis phenotype in N. benthamiana, depending on simultaneous localization to the nuclei and chloroplasts in a BAK1- and SOBIR1-dependent manner. VdScp7, VdGal4, and Vd424y target host cell nuclei to regulate immunity. VdScp41 targets the plant-specific transcription factors CBP60g and SARD1 to modulate immunity. In order to maintain their ability to seize iron, the conserved iron binding site, aspartic acid residue (D), in the common in fungal extracellular membrane structural domain in VdScp76 and VdScp77 was mutated to an asparagine residue (N), which led to a differentiation of the virulence function of the family members, with VdScp76 and VdScp77 being the important virulence factors, and VdScp33, VdScp41, VdScp43, VdScp72, VdScp99, VdScp116, and VdScp120 are synergistically involved in this process. Pevd1 induces ethylene biosynthesis by directly binding to Ore1. VdAve1, VdAmp2, and VdAmp3 target host microbiota to improve infestation capacity. VdAspf2, VdM35-1, VdHp1, VdPel1, and VdCp1 are localized to function within the cell membrane. VdScp27, VdScp113, VdScp126, and VdR3e are localized to function on the cell membrane. VdCe11 targets and interacts with aspartic acid protease (GhAp1) in cotton and promotes the accumulation of GhAp1 and enhances its hydrolase activity, leading to increased susceptibility to V. dahliae. VdEg1 and VdEg3 associate differently with BAK1 and SOBIR1 receptor-like kinases to trigger immunity in N. benthamiana, and together with Cbm1-containing proteins to manipulate plant immunity. VdRtx1 has ribonuclease activity to degrade ribosomal RNA of host plants and is perceived by plant immune system. VdCbm1 suppresses VdEg1, VdEg3, and VdRtx1-induced cell death and some PTI-associated immunity in N. benthamiana