Mutant/mutation
The mutant lacks expression of MAEBL and expresses the fusion protein GFP-Luciferase under control of the constitutive eef1a promoter

Protein (function)
MAEBL is a large type I transmembrane protein composed of two N-terminal cysteine-rich adhesion domains homologous to the apical membrane antigen 1 (AMA-1), named M1 and M2, and a C-terminal cysteine-rich region (C-cys) structurally related with Plasmodium Duffy binding-like family of erythrocyte binding proteins. Conserved among Plasmodium species, MAEBL was initially reported as an erythrocytic-binding protein present in blood-stage parasites, but was later found to be expressed in sporozoites and late liver stages. In sporozoites, MAEBL is found associated with the micronemes. 

Phenotype
Midgut (hemolymph) sporozoites are formed but fail to invade salivary glands. No salivary gland sporozoites. Midgut (hemolymph) sporozoites have reduced infectivity to mice.
Evidence is presented that:
- maebl- hemolymph sporozoites present hampered invasion and wounding of host hapatocytes in vitro
- maebl- hemolymph sporozoites glide at lower average speed and exhibit defective attachment

Additional information
Analyses of a mutant expressing a C-terminal cmyc tagged version of MAEBL (RMgm-5216) showed expression in micronemes of sporozoites (with higher expression in hemolymph sporozoites compared to salivary gland sporozoites). Partial co-localization with thrombospondin related anonymous protein (TRAP) was frequently observed inmidgut and hemolymph sporozoites, confirming themicronemal localization ofMAEBL. However, colocalization with TRAP in salivary gland sporozoites was not as evident in some sporozoites, as TRAPwas frequently found uniformly spread over the sporozoite surface, unlike myc-tagged MAEBL. Immunoelectron microscopy analyses provided evidence that myc-tagged MAEBL was detected not only associated with micronemes but also to the surface of sporozoites, i.e., near the plasma membrane and/or inner membrane complex

Other mutants