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Identification and function of leucine-rich repeat flightless-I-interacting protein 2 (LRRFIP2) in Litopenaeus vannamei.

Zhang S, Yan H, Li CZ, Chen YH, Yuan FH, Chen YG, Weng SP, He JG - PLoS ONE (2013)

Bottom Line: The knockdown of LvLRRFIP2 by RNA interference resulted in higher cumulative mortality of L. vannamei upon V. parahaemolyticus but not S. aureus and WSSV infections.The expression of L. vannamei AMP genes were reduced by dsLvLRRFIP2 interference.These results indicate that LvLRRFIP2 has an important function in antibacterials via the regulation of AMP gene expression.

View Article: PubMed Central - PubMed

Affiliation: Ministry of Education Key Laboratory of Aquatic Product Safety/State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, People's Republic of China.

ABSTRACT
Leucine-rich repeat flightless-I-interacting protein 2 (LRRFIP2) is a myeloid differentiation factor 88-interacting protein with a positive regulatory function in toll-like receptor signaling. In this study, seven LRRFIP2 protein variants (LvLRRFIP2A-G) were identified in Litopenaeus vannamei. All the seven LvLRRFIP2 protein variants encode proteins with a DUF2051 domain. LvLRRFIP2s were upregulated in hemocytes after challenged with lipopolysaccharide, poly I:C, CpG-ODN2006, Vibrio parahaemolyticus, Staphylococcus aureus, and white spot syndrome virus (WSSV). Dual-luciferase reporter assays in Drosophila Schneider 2 cells revealed that LvLRRFIP2 activates the promoters of Drosophila and shrimp AMP genes. The knockdown of LvLRRFIP2 by RNA interference resulted in higher cumulative mortality of L. vannamei upon V. parahaemolyticus but not S. aureus and WSSV infections. The expression of L. vannamei AMP genes were reduced by dsLvLRRFIP2 interference. These results indicate that LvLRRFIP2 has an important function in antibacterials via the regulation of AMP gene expression.

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Multiple sequence alignment of LvLRRFIP2s in Litopenaeus vannamei and phylogenetic analysis of LRRFIP2 proteins from various species.(A) Multiple sequence alignment of LvLRRFIP2s in Litopenaeus vannamei. The identical amino acid residues shaded in black and the similar residues in gray. The DUF2051 domains are boxed. (B) Phylogenetic analysis of LRRFIP2 proteins. A rooted tree was constructed via the neighbor-joining method and was bootstrapped 1000 times using MEGA 4.0 (http://www.megasoftware.net/index.html). LvLRRFIP2 is boxed. LvLRRFIP2, L. vannamei LRRFIP2D (Accession No. JX840476); AeLRRFIP2, Acromyrmex echinatior LRRFIP2 (Accession No. EGI63253); NvLRRFIP2, Nasonia vitripennis LRRFIP2 (Accession No. XP_001608049); LsLRRFIP2; Lepeophtheirus salmonis LRRFIP2 (Accession No. ACO11882); AaLRRFIP2, Aedes aegypti LRRFIP2 (Accession No. XP_001654827); SpLRRFIP2, Strongylocentrotus purpuratus LRRFIP2 (Accession No. XP_782587); IsLRRFIP2, Ixodes scapularis LRRFIP2 (Accession No. XP_002410685); CiLRRFIP2, Ciona intestinalis LRRFIP2 (Accession No. XP_002130672); HsLRRFIP2, Homo sapiens LRRFIP2 (Accession No.NP_060194); BtLRRFIP2, Bos taurus LRRFIP2 (Accession No. NP_001033159); MmLRRFIP2, Mus musculus LRRFIP2 (Accession No. NP_082018); TgLRRFIP2, Taeniopygia guttata LRRFIP2 (Accession No. XP_002198991); DrLRRFIP2, Danio rerio LRRFIP2 (Accession No.NP_955773); XlLRRFIP2, Xenopus laevis LRRFIP2 (Accession No. NP_001085821); OaLRRFIP2, Ornithorhynchus anatinus LRRFIP2 (Accession No. XP_003430994).
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pone-0057456-g001: Multiple sequence alignment of LvLRRFIP2s in Litopenaeus vannamei and phylogenetic analysis of LRRFIP2 proteins from various species.(A) Multiple sequence alignment of LvLRRFIP2s in Litopenaeus vannamei. The identical amino acid residues shaded in black and the similar residues in gray. The DUF2051 domains are boxed. (B) Phylogenetic analysis of LRRFIP2 proteins. A rooted tree was constructed via the neighbor-joining method and was bootstrapped 1000 times using MEGA 4.0 (http://www.megasoftware.net/index.html). LvLRRFIP2 is boxed. LvLRRFIP2, L. vannamei LRRFIP2D (Accession No. JX840476); AeLRRFIP2, Acromyrmex echinatior LRRFIP2 (Accession No. EGI63253); NvLRRFIP2, Nasonia vitripennis LRRFIP2 (Accession No. XP_001608049); LsLRRFIP2; Lepeophtheirus salmonis LRRFIP2 (Accession No. ACO11882); AaLRRFIP2, Aedes aegypti LRRFIP2 (Accession No. XP_001654827); SpLRRFIP2, Strongylocentrotus purpuratus LRRFIP2 (Accession No. XP_782587); IsLRRFIP2, Ixodes scapularis LRRFIP2 (Accession No. XP_002410685); CiLRRFIP2, Ciona intestinalis LRRFIP2 (Accession No. XP_002130672); HsLRRFIP2, Homo sapiens LRRFIP2 (Accession No.NP_060194); BtLRRFIP2, Bos taurus LRRFIP2 (Accession No. NP_001033159); MmLRRFIP2, Mus musculus LRRFIP2 (Accession No. NP_082018); TgLRRFIP2, Taeniopygia guttata LRRFIP2 (Accession No. XP_002198991); DrLRRFIP2, Danio rerio LRRFIP2 (Accession No.NP_955773); XlLRRFIP2, Xenopus laevis LRRFIP2 (Accession No. NP_001085821); OaLRRFIP2, Ornithorhynchus anatinus LRRFIP2 (Accession No. XP_003430994).

Mentions: Seven LvLRRFIP2 variants, namely, LvLRRFIP2A, LvLRRFIP2B, LvLRRFIP2C, LvLRRFIP2D, LvLRRFIP2E, LvLRRFIP2F, and LvLRRFIP2G, were found. The sequences at 5′ end of LvLRRFIP2G were distinct from that of the other six LvLRRFIP2 variants. The 5′ end sequences of LvLRRFIP2A, LvLRRFIP2B, LvLRRFIP2C, and LvLRRFIP2D were identical. Both LvLRRFIP2E and LvLRRFIP2F have the same 5′ end sequences, which were different from that of LvLRRFIP2A-D. The sequence details of these seven variants of LvLRRFIP2 are shown in Fig. S1 and Table 2. Multiple sequence alignment shows that LvLRRFIP2s are highly conserved with each other (Fig. 1A). The amino acid sequence was analyzed using the SMART program to determine the structural domains of LvLRRFIP2. All LvLRRFIP2s have a DUF2051 domain (Fig. 1A), which was found in a dsRNA binding protein named DUF2051, a novel protein that interacts with the LRR domain of human FliI protein [29]. The identities among LvLRRFIP2s ranged from 44% to 97% (Table 3). Compared with the LRRFIP2 proteins from other species, LvLRRFIP2 shares a 35% to 51% identity with the LRRFIP2 proteins from insect to human (Table 4). A phylogenetic tree was constructed to determine the evolutionary relationship of LvLRRFIP2 with other known LRRFIP2 molecules. The phylogenetic tree showed that LvLRRFIP2 belonged to the invertebrate group and was closely related to LRRFIP2 in L. salmonis, Aedes aegypti, Acromyrmex echinatior, Ixodes scapularis, and Nasonia vitripennis, which are all arthropods (Fig. 1B).


Identification and function of leucine-rich repeat flightless-I-interacting protein 2 (LRRFIP2) in Litopenaeus vannamei.

Zhang S, Yan H, Li CZ, Chen YH, Yuan FH, Chen YG, Weng SP, He JG - PLoS ONE (2013)

Multiple sequence alignment of LvLRRFIP2s in Litopenaeus vannamei and phylogenetic analysis of LRRFIP2 proteins from various species.(A) Multiple sequence alignment of LvLRRFIP2s in Litopenaeus vannamei. The identical amino acid residues shaded in black and the similar residues in gray. The DUF2051 domains are boxed. (B) Phylogenetic analysis of LRRFIP2 proteins. A rooted tree was constructed via the neighbor-joining method and was bootstrapped 1000 times using MEGA 4.0 (http://www.megasoftware.net/index.html). LvLRRFIP2 is boxed. LvLRRFIP2, L. vannamei LRRFIP2D (Accession No. JX840476); AeLRRFIP2, Acromyrmex echinatior LRRFIP2 (Accession No. EGI63253); NvLRRFIP2, Nasonia vitripennis LRRFIP2 (Accession No. XP_001608049); LsLRRFIP2; Lepeophtheirus salmonis LRRFIP2 (Accession No. ACO11882); AaLRRFIP2, Aedes aegypti LRRFIP2 (Accession No. XP_001654827); SpLRRFIP2, Strongylocentrotus purpuratus LRRFIP2 (Accession No. XP_782587); IsLRRFIP2, Ixodes scapularis LRRFIP2 (Accession No. XP_002410685); CiLRRFIP2, Ciona intestinalis LRRFIP2 (Accession No. XP_002130672); HsLRRFIP2, Homo sapiens LRRFIP2 (Accession No.NP_060194); BtLRRFIP2, Bos taurus LRRFIP2 (Accession No. NP_001033159); MmLRRFIP2, Mus musculus LRRFIP2 (Accession No. NP_082018); TgLRRFIP2, Taeniopygia guttata LRRFIP2 (Accession No. XP_002198991); DrLRRFIP2, Danio rerio LRRFIP2 (Accession No.NP_955773); XlLRRFIP2, Xenopus laevis LRRFIP2 (Accession No. NP_001085821); OaLRRFIP2, Ornithorhynchus anatinus LRRFIP2 (Accession No. XP_003430994).
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pone-0057456-g001: Multiple sequence alignment of LvLRRFIP2s in Litopenaeus vannamei and phylogenetic analysis of LRRFIP2 proteins from various species.(A) Multiple sequence alignment of LvLRRFIP2s in Litopenaeus vannamei. The identical amino acid residues shaded in black and the similar residues in gray. The DUF2051 domains are boxed. (B) Phylogenetic analysis of LRRFIP2 proteins. A rooted tree was constructed via the neighbor-joining method and was bootstrapped 1000 times using MEGA 4.0 (http://www.megasoftware.net/index.html). LvLRRFIP2 is boxed. LvLRRFIP2, L. vannamei LRRFIP2D (Accession No. JX840476); AeLRRFIP2, Acromyrmex echinatior LRRFIP2 (Accession No. EGI63253); NvLRRFIP2, Nasonia vitripennis LRRFIP2 (Accession No. XP_001608049); LsLRRFIP2; Lepeophtheirus salmonis LRRFIP2 (Accession No. ACO11882); AaLRRFIP2, Aedes aegypti LRRFIP2 (Accession No. XP_001654827); SpLRRFIP2, Strongylocentrotus purpuratus LRRFIP2 (Accession No. XP_782587); IsLRRFIP2, Ixodes scapularis LRRFIP2 (Accession No. XP_002410685); CiLRRFIP2, Ciona intestinalis LRRFIP2 (Accession No. XP_002130672); HsLRRFIP2, Homo sapiens LRRFIP2 (Accession No.NP_060194); BtLRRFIP2, Bos taurus LRRFIP2 (Accession No. NP_001033159); MmLRRFIP2, Mus musculus LRRFIP2 (Accession No. NP_082018); TgLRRFIP2, Taeniopygia guttata LRRFIP2 (Accession No. XP_002198991); DrLRRFIP2, Danio rerio LRRFIP2 (Accession No.NP_955773); XlLRRFIP2, Xenopus laevis LRRFIP2 (Accession No. NP_001085821); OaLRRFIP2, Ornithorhynchus anatinus LRRFIP2 (Accession No. XP_003430994).
Mentions: Seven LvLRRFIP2 variants, namely, LvLRRFIP2A, LvLRRFIP2B, LvLRRFIP2C, LvLRRFIP2D, LvLRRFIP2E, LvLRRFIP2F, and LvLRRFIP2G, were found. The sequences at 5′ end of LvLRRFIP2G were distinct from that of the other six LvLRRFIP2 variants. The 5′ end sequences of LvLRRFIP2A, LvLRRFIP2B, LvLRRFIP2C, and LvLRRFIP2D were identical. Both LvLRRFIP2E and LvLRRFIP2F have the same 5′ end sequences, which were different from that of LvLRRFIP2A-D. The sequence details of these seven variants of LvLRRFIP2 are shown in Fig. S1 and Table 2. Multiple sequence alignment shows that LvLRRFIP2s are highly conserved with each other (Fig. 1A). The amino acid sequence was analyzed using the SMART program to determine the structural domains of LvLRRFIP2. All LvLRRFIP2s have a DUF2051 domain (Fig. 1A), which was found in a dsRNA binding protein named DUF2051, a novel protein that interacts with the LRR domain of human FliI protein [29]. The identities among LvLRRFIP2s ranged from 44% to 97% (Table 3). Compared with the LRRFIP2 proteins from other species, LvLRRFIP2 shares a 35% to 51% identity with the LRRFIP2 proteins from insect to human (Table 4). A phylogenetic tree was constructed to determine the evolutionary relationship of LvLRRFIP2 with other known LRRFIP2 molecules. The phylogenetic tree showed that LvLRRFIP2 belonged to the invertebrate group and was closely related to LRRFIP2 in L. salmonis, Aedes aegypti, Acromyrmex echinatior, Ixodes scapularis, and Nasonia vitripennis, which are all arthropods (Fig. 1B).

Bottom Line: The knockdown of LvLRRFIP2 by RNA interference resulted in higher cumulative mortality of L. vannamei upon V. parahaemolyticus but not S. aureus and WSSV infections.The expression of L. vannamei AMP genes were reduced by dsLvLRRFIP2 interference.These results indicate that LvLRRFIP2 has an important function in antibacterials via the regulation of AMP gene expression.

View Article: PubMed Central - PubMed

Affiliation: Ministry of Education Key Laboratory of Aquatic Product Safety/State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou, People's Republic of China.

ABSTRACT
Leucine-rich repeat flightless-I-interacting protein 2 (LRRFIP2) is a myeloid differentiation factor 88-interacting protein with a positive regulatory function in toll-like receptor signaling. In this study, seven LRRFIP2 protein variants (LvLRRFIP2A-G) were identified in Litopenaeus vannamei. All the seven LvLRRFIP2 protein variants encode proteins with a DUF2051 domain. LvLRRFIP2s were upregulated in hemocytes after challenged with lipopolysaccharide, poly I:C, CpG-ODN2006, Vibrio parahaemolyticus, Staphylococcus aureus, and white spot syndrome virus (WSSV). Dual-luciferase reporter assays in Drosophila Schneider 2 cells revealed that LvLRRFIP2 activates the promoters of Drosophila and shrimp AMP genes. The knockdown of LvLRRFIP2 by RNA interference resulted in higher cumulative mortality of L. vannamei upon V. parahaemolyticus but not S. aureus and WSSV infections. The expression of L. vannamei AMP genes were reduced by dsLvLRRFIP2 interference. These results indicate that LvLRRFIP2 has an important function in antibacterials via the regulation of AMP gene expression.

Show MeSH
Related in: MedlinePlus