Helminth secretomes reflect different lifestyles and parasitized hosts.
Helminths cause a number of medical and agricultural problems and are a major cause of parasitic infections in humans, animals and plants. Comparative analysis of helminth genes and genomes are important to understand the genomic biodiversity and evolution of parasites and their hosts in terms of different selective pressures in their habitats. The interactions between the infective organisms and their hosts are mediated in large part by secreted proteins, known collectively as the "secretome". Proteins secreted by parasites are able to modify a host's environment and modulate their immune system. The composition and function of this set of proteins varies depending on the ecology, lifestyle and environment of an organism. The present study aimed to predict, in silico, the secretome in 44 helminth species including Nematoda (31 species) and Platyhelminthes (13 species) and, understand the diversity and evolution of secretomes. Secretomes from plant helminths range from 7.6% (943 proteins) to 13.9% (2,077 proteins) of the filtered proteome with an average of 10.2% (1,412 proteins) and from free-living helminths range from 4.4% (870 proteins) to 13% (3,121 proteins) with an average of 9.8% (2,126 proteins), respectively, and thus are considerably larger secretomes in relation to animal helminth secretomes which range from 4.2% (431 proteins) to 11.8% (2,419 proteins) of the proteomes, with an average of 7.1% (804 proteins). Across 44 secretomes in different helminth species, we found five conserved domains: (i) PF00014 (Kunitz/Bovine pancreatic trypsin inhibitor domain), (ii) PF00046 (Homeobox domain), (iii) PF00188 (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins), (iv) PF00085 (Thioredoxin) and (v) PF07679 (Immunoglobulin I-set domain). Our results detected secreted proteins associated with invasion, infection, adhesion and immunoregulation processes as protease inhibitors and cytokines, among other functions. In summary, this study will contribute towards the understanding of host-parasite interactions and possibly identify new molecular targets for the treatment or diagnosis of helminthiases.
Centro de Pesquisas René Rachou (CPqRR), Fundação Oswaldo Cruz (FIOCRUZ), Belo Horizonte, MG 30190-002, Brazil; Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais (UFMG), Belo Horizonte, MG 31270-901, Brazil.
Yesid
Y
Cuesta-Astroz
Centro de Pesquisas René Rachou (CPqRR), Fundação Oswaldo Cruz (FIOCRUZ), Belo Horizonte, MG 30190-002, Brazil; Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais (UFMG), Belo Horizonte, MG 31270-901, Brazil.
Francislon Silva de
FS
Oliveira
Centro de Pesquisas René Rachou (CPqRR), Fundação Oswaldo Cruz (FIOCRUZ), Belo Horizonte, MG 30190-002, Brazil; Faculdade Promove de Tecnologia, Belo Horizonte, MG 30130-180, Brazil.
Laila Alves
LA
Nahum
Centro de Pesquisas René Rachou (CPqRR), Fundação Oswaldo Cruz (FIOCRUZ), Belo Horizonte, MG 30190-002, Brazil; Instituto Tecnológico Vale, Belém, PA 66055-090, Brazil. Electronic address: guilherme.oliveira@itv.org.
Guilherme
G
Oliveira
D000818:Animals; D044822:Biodiversity; D017124:Conserved Sequence; D016678:Genome; D015801:Helminth Proteins / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D006376:Helminths / Q000145:classification / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D006790:Host-Parasite Interactions; D008019:Life Style; D010802:Phylogeny; D010944:Plants / Q000469:parasitology; D000072417:Protein Domains; D021382:Protein Sorting Signals / Q000502:physiology; D013045:Species Specificity
D015801:Helminth Proteins; D021382:Protein Sorting Signals
Biodiversity; Computational biology; Helminths; Host-parasite interaction; Protein evolution; Secretome