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Bacteria-Induced Dscam Isoforms of the Crustacean, Pacifastacus leniusculus.

Watthanasurorot A, Jiravanichpaisal P, Liu H, Söderhäll I, Söderhäll K - PLoS Pathog. (2011)

Bottom Line: The cytoplasmic tail can generate multiple isoforms.PlDscam can generate more than 22,000 different unique isoforms.Furthermore, PlDscam silencing did not have any effect on the replication of the WSSV.

View Article: PubMed Central - PubMed

Affiliation: Department of Comparative Physiology, Uppsala University, Uppsala, Sweden.

ABSTRACT
The Down syndrome cell adhesion molecule, also known as Dscam, is a member of the immunoglobulin super family. Dscam plays an essential function in neuronal wiring and appears to be involved in innate immune reactions in insects. The deduced amino acid sequence of Dscam in the crustacean Pacifastacus leniusculus (PlDscam), encodes 9(Ig)-4(FNIII)-(Ig)-2(FNIII)-TM and it has variable regions in the N-terminal half of Ig2 and Ig3 and the complete Ig7 and in the transmembrane domain. The cytoplasmic tail can generate multiple isoforms. PlDscam can generate more than 22,000 different unique isoforms. Bacteria and LPS injection enhanced the expression of PlDscam, but no response in expression occurred after a white spot syndrome virus (WSSV) infection or injection with peptidoglycans. Furthermore, PlDscam silencing did not have any effect on the replication of the WSSV. Bacterial specific isoforms of PlDscam were shown to have a specific binding property to each tested bacteria, E. coli or S. aureus. The bacteria specific isoforms of PlDscam were shown to be associated with bacterial clearance and phagocytosis in crayfish.

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Related in: MedlinePlus

Identification and characterization of Dscam in P. leniusculus.A) Amino acid sequence of PlDscam; double underlining represents signal peptide, while the Immunoglobulin (Ig) and Fibronectin type III (FNIII) domains are indicated by light and dark gray shading, respectively. A conserved RGD motif between Ig6 and Ig7 is indicated by single underlining. In addition, the single transmembrane domain is shown in a box. B) Schematic diagram showing the domain organization of the PlDscam protein. C) 3′ UTR containing the polyadenylation signal (AATAA) is indicated by double underlining and a stop codon is bold and underlined.
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ppat-1002062-g001: Identification and characterization of Dscam in P. leniusculus.A) Amino acid sequence of PlDscam; double underlining represents signal peptide, while the Immunoglobulin (Ig) and Fibronectin type III (FNIII) domains are indicated by light and dark gray shading, respectively. A conserved RGD motif between Ig6 and Ig7 is indicated by single underlining. In addition, the single transmembrane domain is shown in a box. B) Schematic diagram showing the domain organization of the PlDscam protein. C) 3′ UTR containing the polyadenylation signal (AATAA) is indicated by double underlining and a stop codon is bold and underlined.

Mentions: A large open reading frame of PlDscam (6,009 bp) was identified that encodes a polypeptide of 2,002 aa (Figure 1A). The closest sequence matching that of PlDscam was Dscam of L. vannamei (identity  = 85%). Domain homology analysis using SMART showed that the deduced amino acid sequence contains a signal peptide at amino acids 1–24, ten tandem repeated immunoglobulin domains (Ig), six fibronectin type III domains (FNIII) and a transmembrane domain (TM). The domain organization of PlDscam is 9(Ig)-4(FNIII)-(Ig)-2(FNIII)-TM (Figure 1B). It also has a conserved cell attachment sequence (Arg-Gly-Asp: RGD motif) between Ig6 and Ig7 (Figure 1A). The sequence in the 3′ UTR contains a polyadenylation signal (AATAA) and is located at 55 bp upstream of the poly A tail (Figure 1C).


Bacteria-Induced Dscam Isoforms of the Crustacean, Pacifastacus leniusculus.

Watthanasurorot A, Jiravanichpaisal P, Liu H, Söderhäll I, Söderhäll K - PLoS Pathog. (2011)

Identification and characterization of Dscam in P. leniusculus.A) Amino acid sequence of PlDscam; double underlining represents signal peptide, while the Immunoglobulin (Ig) and Fibronectin type III (FNIII) domains are indicated by light and dark gray shading, respectively. A conserved RGD motif between Ig6 and Ig7 is indicated by single underlining. In addition, the single transmembrane domain is shown in a box. B) Schematic diagram showing the domain organization of the PlDscam protein. C) 3′ UTR containing the polyadenylation signal (AATAA) is indicated by double underlining and a stop codon is bold and underlined.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3111544&req=5

ppat-1002062-g001: Identification and characterization of Dscam in P. leniusculus.A) Amino acid sequence of PlDscam; double underlining represents signal peptide, while the Immunoglobulin (Ig) and Fibronectin type III (FNIII) domains are indicated by light and dark gray shading, respectively. A conserved RGD motif between Ig6 and Ig7 is indicated by single underlining. In addition, the single transmembrane domain is shown in a box. B) Schematic diagram showing the domain organization of the PlDscam protein. C) 3′ UTR containing the polyadenylation signal (AATAA) is indicated by double underlining and a stop codon is bold and underlined.
Mentions: A large open reading frame of PlDscam (6,009 bp) was identified that encodes a polypeptide of 2,002 aa (Figure 1A). The closest sequence matching that of PlDscam was Dscam of L. vannamei (identity  = 85%). Domain homology analysis using SMART showed that the deduced amino acid sequence contains a signal peptide at amino acids 1–24, ten tandem repeated immunoglobulin domains (Ig), six fibronectin type III domains (FNIII) and a transmembrane domain (TM). The domain organization of PlDscam is 9(Ig)-4(FNIII)-(Ig)-2(FNIII)-TM (Figure 1B). It also has a conserved cell attachment sequence (Arg-Gly-Asp: RGD motif) between Ig6 and Ig7 (Figure 1A). The sequence in the 3′ UTR contains a polyadenylation signal (AATAA) and is located at 55 bp upstream of the poly A tail (Figure 1C).

Bottom Line: The cytoplasmic tail can generate multiple isoforms.PlDscam can generate more than 22,000 different unique isoforms.Furthermore, PlDscam silencing did not have any effect on the replication of the WSSV.

View Article: PubMed Central - PubMed

Affiliation: Department of Comparative Physiology, Uppsala University, Uppsala, Sweden.

ABSTRACT
The Down syndrome cell adhesion molecule, also known as Dscam, is a member of the immunoglobulin super family. Dscam plays an essential function in neuronal wiring and appears to be involved in innate immune reactions in insects. The deduced amino acid sequence of Dscam in the crustacean Pacifastacus leniusculus (PlDscam), encodes 9(Ig)-4(FNIII)-(Ig)-2(FNIII)-TM and it has variable regions in the N-terminal half of Ig2 and Ig3 and the complete Ig7 and in the transmembrane domain. The cytoplasmic tail can generate multiple isoforms. PlDscam can generate more than 22,000 different unique isoforms. Bacteria and LPS injection enhanced the expression of PlDscam, but no response in expression occurred after a white spot syndrome virus (WSSV) infection or injection with peptidoglycans. Furthermore, PlDscam silencing did not have any effect on the replication of the WSSV. Bacterial specific isoforms of PlDscam were shown to have a specific binding property to each tested bacteria, E. coli or S. aureus. The bacteria specific isoforms of PlDscam were shown to be associated with bacterial clearance and phagocytosis in crayfish.

Show MeSH
Related in: MedlinePlus