Limits...
Evolution and Structural Analyses of Glossina morsitans (Diptera; Glossinidae) Tetraspanins.

Murungi EK, Kariithi HM, Adunga V, Obonyo M, Christoffels A - Insects (2014)

Bottom Line: Here, we report that the genome of the tsetse fly, Glossina morsitans (Diptera: Glossinidae) encodes at least seventeen tetraspanins (GmTsps), all containing the signature features found in the tetraspanin superfamily members.Whereas six of the GmTsps have been previously reported, eleven could be classified as novel because their amino acid sequences do not map to characterized tetraspanins in the available protein data bases.Structurally, the GmTsps are largely similar to vertebrate tetraspanins.

View Article: PubMed Central - PubMed

Affiliation: South African National Bioinformatics Institute (SANBI), University of the Western Cape, Private Bag X79, Bellville, Cape Town 7535, South Africa. eddkimm@gmail.com.

ABSTRACT
Tetraspanins are important conserved integral membrane proteins expressed in many organisms. Although there is limited knowledge about the full repertoire, evolution and structural characteristics of individual members in various organisms, data obtained so far show that tetraspanins play major roles in membrane biology, visual processing, memory, olfactory signal processing, and mechanosensory antennal inputs. Thus, these proteins are potential targets for control of insect pests. Here, we report that the genome of the tsetse fly, Glossina morsitans (Diptera: Glossinidae) encodes at least seventeen tetraspanins (GmTsps), all containing the signature features found in the tetraspanin superfamily members. Whereas six of the GmTsps have been previously reported, eleven could be classified as novel because their amino acid sequences do not map to characterized tetraspanins in the available protein data bases. We present a model of the GmTsps by using GmTsp42Ed, whose presence and expression has been recently detected by transcriptomics and proteomics analyses of G. morsitans. Phylogenetically, the identified GmTsps segregate into three major clusters. Structurally, the GmTsps are largely similar to vertebrate tetraspanins. In view of the exploitation of tetraspanins by organisms for survival, these proteins could be targeted using specific antibodies, recombinant large extracellular loop (LEL) domains, small-molecule mimetics and siRNAs as potential novel and efficacious putative targets to combat African trypanosomiasis by killing the tsetse fly vector.

No MeSH data available.


Related in: MedlinePlus

Ramachandran plots for GmTsp42Ed: The plot statistics are indicated for all the non-glycine and non-proline residues that fell within the favored regions. Shown in red, yellow, pale yellow, and white, respectively, are amino acid residues in most favored, additionally allowed, generously allowed, and disallowed regions. Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater that 20%, a good model is expected to have ≥90% in the most favored regions. The plots were generated using PROCHECK v. 3.5.4 [66].
© Copyright Policy
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4592607&req=5

insects-05-00885-f005: Ramachandran plots for GmTsp42Ed: The plot statistics are indicated for all the non-glycine and non-proline residues that fell within the favored regions. Shown in red, yellow, pale yellow, and white, respectively, are amino acid residues in most favored, additionally allowed, generously allowed, and disallowed regions. Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater that 20%, a good model is expected to have ≥90% in the most favored regions. The plots were generated using PROCHECK v. 3.5.4 [66].

Mentions: We stereochemically ascertained the quality and accuracy of the GmTsp42Ed using the PROCHECK protein structure validation and verification package. The Ramachandran plot obtained showed that 87.8%, 7.3%, 2.9%, and 2.0% of residues fell within the most favored regions, additionally favored regions, generously allowed regions and the disallowed regions, respectively (Figure 5). This makes a combined percentage of 98.0% of the residues in the favored and allowed regions for the model making it stereochemically robust [86]. Again, using GmTsp42Ed as a representative of G. morsitans tetraspanins, this result appears to confirm that in general, the GmTsps belong to the tetraspanin superfamily.


Evolution and Structural Analyses of Glossina morsitans (Diptera; Glossinidae) Tetraspanins.

Murungi EK, Kariithi HM, Adunga V, Obonyo M, Christoffels A - Insects (2014)

Ramachandran plots for GmTsp42Ed: The plot statistics are indicated for all the non-glycine and non-proline residues that fell within the favored regions. Shown in red, yellow, pale yellow, and white, respectively, are amino acid residues in most favored, additionally allowed, generously allowed, and disallowed regions. Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater that 20%, a good model is expected to have ≥90% in the most favored regions. The plots were generated using PROCHECK v. 3.5.4 [66].
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4592607&req=5

insects-05-00885-f005: Ramachandran plots for GmTsp42Ed: The plot statistics are indicated for all the non-glycine and non-proline residues that fell within the favored regions. Shown in red, yellow, pale yellow, and white, respectively, are amino acid residues in most favored, additionally allowed, generously allowed, and disallowed regions. Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater that 20%, a good model is expected to have ≥90% in the most favored regions. The plots were generated using PROCHECK v. 3.5.4 [66].
Mentions: We stereochemically ascertained the quality and accuracy of the GmTsp42Ed using the PROCHECK protein structure validation and verification package. The Ramachandran plot obtained showed that 87.8%, 7.3%, 2.9%, and 2.0% of residues fell within the most favored regions, additionally favored regions, generously allowed regions and the disallowed regions, respectively (Figure 5). This makes a combined percentage of 98.0% of the residues in the favored and allowed regions for the model making it stereochemically robust [86]. Again, using GmTsp42Ed as a representative of G. morsitans tetraspanins, this result appears to confirm that in general, the GmTsps belong to the tetraspanin superfamily.

Bottom Line: Here, we report that the genome of the tsetse fly, Glossina morsitans (Diptera: Glossinidae) encodes at least seventeen tetraspanins (GmTsps), all containing the signature features found in the tetraspanin superfamily members.Whereas six of the GmTsps have been previously reported, eleven could be classified as novel because their amino acid sequences do not map to characterized tetraspanins in the available protein data bases.Structurally, the GmTsps are largely similar to vertebrate tetraspanins.

View Article: PubMed Central - PubMed

Affiliation: South African National Bioinformatics Institute (SANBI), University of the Western Cape, Private Bag X79, Bellville, Cape Town 7535, South Africa. eddkimm@gmail.com.

ABSTRACT
Tetraspanins are important conserved integral membrane proteins expressed in many organisms. Although there is limited knowledge about the full repertoire, evolution and structural characteristics of individual members in various organisms, data obtained so far show that tetraspanins play major roles in membrane biology, visual processing, memory, olfactory signal processing, and mechanosensory antennal inputs. Thus, these proteins are potential targets for control of insect pests. Here, we report that the genome of the tsetse fly, Glossina morsitans (Diptera: Glossinidae) encodes at least seventeen tetraspanins (GmTsps), all containing the signature features found in the tetraspanin superfamily members. Whereas six of the GmTsps have been previously reported, eleven could be classified as novel because their amino acid sequences do not map to characterized tetraspanins in the available protein data bases. We present a model of the GmTsps by using GmTsp42Ed, whose presence and expression has been recently detected by transcriptomics and proteomics analyses of G. morsitans. Phylogenetically, the identified GmTsps segregate into three major clusters. Structurally, the GmTsps are largely similar to vertebrate tetraspanins. In view of the exploitation of tetraspanins by organisms for survival, these proteins could be targeted using specific antibodies, recombinant large extracellular loop (LEL) domains, small-molecule mimetics and siRNAs as potential novel and efficacious putative targets to combat African trypanosomiasis by killing the tsetse fly vector.

No MeSH data available.


Related in: MedlinePlus