Philippe Barthe

1 Introduction The Apicomplexa constitute a large group of single-celled eukaryotic parasites, which are highly host specific and have a complex life cycle to enable invasion. They are obligate intracellular parasites, with at least one developmental stage requiring a host cell. The Apicomplexa infect only eukaryotic cells, mostly of mammalian origin, though some use insects or acarians as vectors [1].

Abstract Magnaporthe AVRs and ToxB-like (MAX) effectors constitute a family of secreted virulence proteins in the fungus Pyricularia oryzae (syn. Magnaporthe oryzae), which causes blast disease on numerous cereals and grasses. In spite of high sequence divergence, MAX effectors share a common fold characterized by a β-sandwich core stabilized by a conserved disulfide bond. In this study, we investigated the structural landscape and diversity within the MAX effector repertoire of P. oryzae.

Abstract Plant pathogenic fungi secrete a wide variety of small proteins, named effectors. Magnaporthe AVRs and ToxB-like (MAX) effectors constitute a superfamily of secreted proteins widely distributed in Pyricularia (syn. Magnaporthe) oryzae, a devastating fungus responsible for blast disease in cereals such as rice. In spite of high evolutionary sequence divergence, MAX effectors share a common fold characterized by a β-sandwich core often stabilized by a conserved disulfide bond.