Table 3

Putative immune regulatory genes of L. striatellus that might be involved in resistance to viral infection.

Regulatory protein

Function and description

Code of ESTs (e-value)


RNAi systems

Dicer like protein

RNAIII family endo-ribonucleases that cleave double-stranded RNA and pre-microRNA into short dsRNA fragments.

Contig2793 (2e-27), Contig6128 (6e-06),

FQ4QJ5301BI24S (6e-17),

FQ92HJ001CXB6B (2e-13),

FQ4QJ5301EGA00 (7e-09)

Argonaute like protein

Catalytic component of the RNA-induced silencing complex

Contig1164 (7e-24), Contig6509 (2e-18),

Contig15043 (2e-21),

FQ4QJ5301BLRSO (5e-38),

FQ92HJ001AVX3O (4e-16),

Q92HJ001B74KA (1e-10),

FQ92HJ001DDNCB (1e-11)

R2D2

dsRNA-binding proteins

No matchb

R3D1

dsRNA-binding proteins

FQ92HJ001EMI2C (1e-05)

JAK/STAT pathway

UPD-like protein

Ligand activating JAK/STAT pathway

No matchb

Domeless

Transmembrane cytokine receptor

FQ92HJ001EGTO6 (0.99)

Hopscotch

Janus Kinases (JAK) that have tyrosine kinase activity

Not determined c

STAT

SH2-domain containing protein that can be phosphorylated by JAK

FQ4QJ5301ERDD2 (1e-15)

Imd pathway

Imd

Death domain-containing protein that similar to receptor interacting protein (RIP) of TNF-R pathway

FQ92HJ001A68SH (0.031)

PGRP

Peptidoglycan recognition protein

Contig145 (6e-23), Contig6140 (1e-26),

Contig6821 (3e-37)

Relish a

NF-κB-like transcription factor

FQ4QJ5301E34NM (0.014)

MAP3K, TAK1

Mitogen-activated protein 3 kinase

Not determined c

TAB2

TAK1 binding protein

FQ4QJ5301DF7ET (1e-18)

DIAP2

Inhibitor of apoptosis proteins

Contig3110 (1e-21)

IKKβ/ird5

Inhibitor of NF-κB kinase

Not determined c

IKKγ/Kenny

Inhibitor of NF-κB kinase

Not determined c

dFADD

Fas-associated death domain protein

FQ92HJ001A68SH (0.031)

Dredd caspase

A caspase involved in apoptosis

No matchb


a. The protein Relish is usually regarded as a component of the NF-κB pathway.

b. No significant match (e ≤ 10-3) in searching EST libraries of L. striatellus.

c. This indicates that although there are significant matches, but it is hard to determine the preferred one since these matched proteins are highly similar in predicted secondary structure.

Zhang et al. BMC Genomics 2010 11:303   doi:10.1186/1471-2164-11-303

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