Cloning and molecular characterization of two invertebrate‐type lysozymes from <i>Anopheles gambiae</i>

Paskewitz, Susan M.; Li, B.; Kajla, Mayur K.

doi:10.1111/j.1365-2583.2008.00797.x

Cited by 33 publications

(32 citation statements)

References 44 publications

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“…However, this is not the case in some other predicted i-type lysozymes. Whether these enzymes are inactive, or whether this glutamic acid residue is not essential for their lysozyme activity, is not yet clear, but site-directed mutagenesis confi rmed the catalytic importance of Glu18 in TjL (Goto et al 2007;Paskewitz et al 2008). In the spatial structure of TjL, Asp30, which is also well conserved in i-type lysozymes, is proximal to Glu18 and, therefore, was presumed to function in the same way as Asp52 in HEWL.…”

Section: Catalytic Mechanismmentioning

confidence: 96%

“…In humans and mice, the g-type lysozymes exhibit tissue-dependent expression (Irwin and Gong 2003; cfr section 5). To date, the presence of multiple i-type lysozymes has been reported for a few mollusk species (Ito et al 1999;Olsen et al 2003;Xue et al 2004; Xue et al 2007; Itoh and Takahashi 2007), the mosquito Anopheles gambiae (Paskewitz et al 2008) and the medical leech Hirudo medicinalis (Zavalova et al 1996(Zavalova et al , 2000.…”

Section: Genomic Organization and Evolution Of Lysozyme Genesmentioning

confidence: 97%

“…The N-terminal sequence (11 amino acids) and the C-terminal sequence (2 amino acids) might be processed in vivo. For other itype lysozymes, signal sequences with great variability in length and sequence are predicted (Bachali et al 2002(Bachali et al , 2004Olsen et al 2003;Itoh and Takahashi 2007;Xue et al 2007;Paskewitz et al 2008), and comparison of the predicted protein sequences from cDNA with the mature protein reveals, for some lysozymes, an additional region at the N-terminal end, which is thought to be cleaved off from a possibly inactive pro-form (Olsen et al 2003;Bachali et al 2004;Paskewitz et al 2008).…”

Section: I-type Lysozymesmentioning

confidence: 99%

“…Reports of similarity searches and our own BLAST searches reveal putative i-type lysozymes in the Annelida, Echinodermata, Crustacea, Insects, Mollusca and Nematoda (Ito et al 1999;Paskewitz et al 2008;www.ncbi.nlm.nih.gov/, December 2009 Urochordates Ciona intestinalis cDNA (EST) isolation Irwin and Gong 2003;Nilsen et al 2003 Oikopleura dioica cDNA (EST) isolation Irwin and Gong 2003;Nilsen et al 2003 1 Destabilase is an enzyme that hydrolyses isopeptide bonds formed between a glutamine γ-carboxamide and a lysine ε-amino group. In the leech, destabilase has been known for a long time as the enzyme in the salivary gland secretion that prevents ingested blood from clotting (Baskova and Nikonov 1991).…”

Section: I-type Lysozymesmentioning

confidence: 99%

“…Typical g-type lysozymes are signifi cantly larger (~20-22 kDa) than c-and i-type lysozymes (~11-15 kDa). In general, c-and g-type lysozymes are basic proteins; this is refl ected in their high isoelectric point (pI) values, while i-type lysozymes Eisenia foetida Earthworm N-terminal AA sequence Ito et al 1999 Medicinal leech Experimental evidence for lytic activity of the destabilase protein Zavalova et al 2000;Zavalova et al 2004 Nephthys hombergi N-terminal AA sequence Périn and Jollès 1972 Arthropoda Anopheles gambiae (mosquito) cDNA isolation Paskewitz et al 2008 Echinodermata Sea cucumber cDNA isolation Cong et al 2009 Starfi sh cDNA isolation and AA sequence Bachali et al 2004 Mollusks Tapes japonica cDNA isolation and AA sequence Ito et al 1999;Takeshita et al 2004 Chlamys islandica cDNA isolation Nilsen et al 1999 6 bivalve species, e.g. Mytilus edulis cDNA isolation Bachali et al 2002 Crassostrea gigas cDNA isolation Matsumoto et al 2006;Itoh and Takahashi 2007 Ostrea edulis cDNA isolation Matsumoto et al 2006 Crassostrea virginica cDNA isolation Xue et al 2007 Lunella coronata Marine conch N-terminal AA sequence Ito et al 1999 Purple washington clam Saxidomus purpurata N-terminal AA sequence Miyauchi et al 2006 Porifera Suberites domuncula cDNA isolation Thakur et al 2005 have quite variable pIs (Xue et al 2004).…”

Section: I-type Lysozymesmentioning

confidence: 99%

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Lysozymes in the animal kingdom

2010

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Lysozymes (EC 3.2.1.17) are hydrolytic enzymes, characterized by their ability to cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, the major bacterial cell wall polymer. In the animal kingdom, three major distinct lysozyme types have been identified--the c-type (chicken or conventional type), the g-type (goose-type) and the i-type (invertebrate type) lysozyme. Examination of the phylogenetic distribution of these lysozymes reveals that c-type lysozymes are predominantly present in the phylum of the Chordata and in different classes of the Arthropoda. Moreover, g-type lysozymes (or at least their corresponding genes) are found in members of the Chordata, as well as in some bivalve mollusks belonging to the invertebrates. In general, the latter animals are known to produce i-type lysozymes. Although the homology in primary structure for representatives of these three lysozyme types is limited, their three-dimensional structures show striking similarities. Nevertheless, some variation exists in their catalytic mechanisms and the genomic organization of their genes. Regarding their biological role, the widely recognized function of lysozymes is their contribution to antibacterial defence but, additionally, some lysozymes (belonging to different types) are known to function as digestive enzymes.

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Section: Catalytic Mechanismmentioning

confidence: 96%