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Sarcoptes scabiei: genomics to proteomics to biology.

Arlian LG, Morgan MS, Rider SD - Parasit Vectors (2016)

Bottom Line: An annotated genome of Sarcoptes scabiei var. canis has been deposited in the National Center for Biotechnology Information (NCBI) and VectorBase and a proteomic analysis of proteins in extracts of mite bodies and eggs from this strain has been reported.Here we mined the data to identify predicted proteins that are known to be involved in specific biological processes in other animals.This analysis helps understand the biology of Sarcoptes scabiei var. canis and adds to the data already available in NCBI and VectorBase.

View Article: PubMed Central - PubMed

Affiliation: Department of Biological Sciences, Wright State University, 3640 Colonel Glenn Hwy, Dayton, OH, 45435, USA. larry.arlian@wright.edu.

ABSTRACT

Background: The common scabies mite, Sarcoptes scabiei is a cosmopolitan parasite of humans and other mammals. An annotated genome of Sarcoptes scabiei var. canis has been deposited in the National Center for Biotechnology Information (NCBI) and VectorBase and a proteomic analysis of proteins in extracts of mite bodies and eggs from this strain has been reported. Here we mined the data to identify predicted proteins that are known to be involved in specific biological processes in other animals.

Results: We identified predicted proteins that are associated with immunomodulation of the host defense system, and biological processes of the mite including oxygen procurement and aerobic respiration, oxidative metabolism, sensory reception and locating a host, neuronal transmission, stressors (heat shock proteins), molting, movement, nutrient procurement and digestion, and excretion and water balance. We used these data to speculate that certain biological processes may occur in scabies mites.

Conclusion: This analysis helps understand the biology of Sarcoptes scabiei var. canis and adds to the data already available in NCBI and VectorBase.

No MeSH data available.


Related in: MedlinePlus

Neighbor joining tree of cysteine protease homologs. Asterisks indicate those containing active site residues that are intact. Accessions beginning with “A” are Sarcoptes scabiei var. hominis, and those with “K” are S. scabiei var. canis. All putatively active members cluster together
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Fig2: Neighbor joining tree of cysteine protease homologs. Asterisks indicate those containing active site residues that are intact. Accessions beginning with “A” are Sarcoptes scabiei var. hominis, and those with “K” are S. scabiei var. canis. All putatively active members cluster together

Mentions: Scabies mites collected from human patients have previously been reported to possess a single, active Sar s 3 homolog and 16 structurally similar proteins (designated as Scabies Mite Inactivated Protease Paralogs or SMIPP-S) in which the catalytic triad is mutated so as to make them inactive [64]. The active protease is reported to be a digestive enzyme that is able to partially digest filaggrin, a protein found in human skin [65], while some of the inactive paralogs can inhibit the human complement system, presumably playing a role in allowing the parasite to evade the host’s immune defense systems [16]. Examination of the structures predicted for the various serine proteases of S. scabiei var. canis revealed that only five of 13 trypsin-like serine proteases, five of 10 serine protease-like proteins and two of the 18 Sar s 3 serine protease-like proteins had intact catalytic triads while the other members of these three groups of proteins had mutations similar to those in the SMIPP-S proteins (Additional file 1: Table S13). Phylogenetic comparisons of the Sar s 3 homologs from both human and dog scabies mites indicated that the sequences in both lineages that contain an active catalytic triad are derived from a common ancestral gene (Fig. 1). The remaining inactive protease genes appear to have undergone duplications and acquired inactivating mutations both before and after the split between the two mite lineages. Additionally, most of the mutant S. scabiei var. canis proteins did have intact substrate-binding sites. In the case of the ten predicted Sar s 1 cysteine protease-like proteins, five (KPM05039 – KPM05043) had intact catalytic triads and were orthologs of previously-reported Sar s 1 proteins (AAS93667–AAS93671) [66], suggesting an ancient and essential function for these five proteins (Fig. 2). The other five Sar s 1 family members had mutations in the catalytic triad like those in the SMIPP-C protein group, but the relationships of the S. scabiei var. canis homologs to those found in human scabies mites suggest that both recent and ancient duplications have occurred in the two scabies mite lineages.Fig. 1


Sarcoptes scabiei: genomics to proteomics to biology.

Arlian LG, Morgan MS, Rider SD - Parasit Vectors (2016)

Neighbor joining tree of cysteine protease homologs. Asterisks indicate those containing active site residues that are intact. Accessions beginning with “A” are Sarcoptes scabiei var. hominis, and those with “K” are S. scabiei var. canis. All putatively active members cluster together
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4930577&req=5

Fig2: Neighbor joining tree of cysteine protease homologs. Asterisks indicate those containing active site residues that are intact. Accessions beginning with “A” are Sarcoptes scabiei var. hominis, and those with “K” are S. scabiei var. canis. All putatively active members cluster together
Mentions: Scabies mites collected from human patients have previously been reported to possess a single, active Sar s 3 homolog and 16 structurally similar proteins (designated as Scabies Mite Inactivated Protease Paralogs or SMIPP-S) in which the catalytic triad is mutated so as to make them inactive [64]. The active protease is reported to be a digestive enzyme that is able to partially digest filaggrin, a protein found in human skin [65], while some of the inactive paralogs can inhibit the human complement system, presumably playing a role in allowing the parasite to evade the host’s immune defense systems [16]. Examination of the structures predicted for the various serine proteases of S. scabiei var. canis revealed that only five of 13 trypsin-like serine proteases, five of 10 serine protease-like proteins and two of the 18 Sar s 3 serine protease-like proteins had intact catalytic triads while the other members of these three groups of proteins had mutations similar to those in the SMIPP-S proteins (Additional file 1: Table S13). Phylogenetic comparisons of the Sar s 3 homologs from both human and dog scabies mites indicated that the sequences in both lineages that contain an active catalytic triad are derived from a common ancestral gene (Fig. 1). The remaining inactive protease genes appear to have undergone duplications and acquired inactivating mutations both before and after the split between the two mite lineages. Additionally, most of the mutant S. scabiei var. canis proteins did have intact substrate-binding sites. In the case of the ten predicted Sar s 1 cysteine protease-like proteins, five (KPM05039 – KPM05043) had intact catalytic triads and were orthologs of previously-reported Sar s 1 proteins (AAS93667–AAS93671) [66], suggesting an ancient and essential function for these five proteins (Fig. 2). The other five Sar s 1 family members had mutations in the catalytic triad like those in the SMIPP-C protein group, but the relationships of the S. scabiei var. canis homologs to those found in human scabies mites suggest that both recent and ancient duplications have occurred in the two scabies mite lineages.Fig. 1

Bottom Line: An annotated genome of Sarcoptes scabiei var. canis has been deposited in the National Center for Biotechnology Information (NCBI) and VectorBase and a proteomic analysis of proteins in extracts of mite bodies and eggs from this strain has been reported.Here we mined the data to identify predicted proteins that are known to be involved in specific biological processes in other animals.This analysis helps understand the biology of Sarcoptes scabiei var. canis and adds to the data already available in NCBI and VectorBase.

View Article: PubMed Central - PubMed

Affiliation: Department of Biological Sciences, Wright State University, 3640 Colonel Glenn Hwy, Dayton, OH, 45435, USA. larry.arlian@wright.edu.

ABSTRACT

Background: The common scabies mite, Sarcoptes scabiei is a cosmopolitan parasite of humans and other mammals. An annotated genome of Sarcoptes scabiei var. canis has been deposited in the National Center for Biotechnology Information (NCBI) and VectorBase and a proteomic analysis of proteins in extracts of mite bodies and eggs from this strain has been reported. Here we mined the data to identify predicted proteins that are known to be involved in specific biological processes in other animals.

Results: We identified predicted proteins that are associated with immunomodulation of the host defense system, and biological processes of the mite including oxygen procurement and aerobic respiration, oxidative metabolism, sensory reception and locating a host, neuronal transmission, stressors (heat shock proteins), molting, movement, nutrient procurement and digestion, and excretion and water balance. We used these data to speculate that certain biological processes may occur in scabies mites.

Conclusion: This analysis helps understand the biology of Sarcoptes scabiei var. canis and adds to the data already available in NCBI and VectorBase.

No MeSH data available.


Related in: MedlinePlus