Characterization of a Novel Lysozyme-Like 4 Gene in the Rat

Narmadha, Ganapathy; Muneswararao, Katakam; Angireddy, Rajesh; Yenugu, Suresh

doi:10.1371/journal.pone.0027659

Cited by 15 publications

(26 citation statements)

References 30 publications

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“…32 A review of the literature reveals that two residues of human lysozyme are replaced in SLLP1, resulting in a loss of the bacteriolytic activity. Similar reports have also been found for mouse LYZL4, 7 and rat LYZL4, 33 because of the replacement of aspartate by glycine at the catalytic site. We therefore consider that the two catalytic residues are necessary for protein bacteriolytic activity.…”

Section: Characterisation Of Lyzlssupporting

confidence: 85%

Characterisation of Lyzls in mice and antibacterial properties of human LYZL6

Wei

Li²,

Shi³

et al. 2013

Asian J Androl

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C-type lysozyme genes (Lyzls) belong to the class of lysozymes and are highly expressed in the testis and epididymis. The members Lyzl4 and Spaca3 have been reported to play a role in sperm-egg binding and fertilisation in mice. However, the function of the remaining two mouse c-type lysozyme genes, Lyzl1 and Lyzl6, is still not clear. In the present study, we analysed the tissue expression and androgen-dependent expression of mouse c-type lysozyme genes and the possible contribution of human recombinant LYZL6 (rLYZL6) to immunity. The expression of Lyzls was detected by RT-PCR, Western blots, immunohistochemistry and immunofluorescence. The bacteriolytic activity of rLYZL6 was analysed by a colony-forming assay. In mice, the expression of Lyzl genes was mainly in the testis and epididymis in a developmentally regulated manner and androgen-or testicular factor-regulated manner. Immunodetection revealed the presence of LYZL6 protein in primary spermatocytes and round spermatids of the testis and on the post-acrosomal area and midpiece of mature epididymal spermatozoa. The rLYZL6 protein exhibited antibacterial activity. From the results, Lyzls may play a role in mitochondrial function of spermatozoa and LYZL6 may contribute to the innate immunity of the male genital tract.

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Section: Characterisation Of Lyzlssupporting

confidence: 85%

Characterisation of Lyzls in mice and antibacterial properties of human LYZL6

Wei

Li²,

Shi³

et al. 2013

Asian J Androl

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show abstract

“…In order to determine the role of LYZL proteins in male reproduction in this study, we report the expression pattern of two additional rat Lyzl transcripts and proteins and present the results in combination with those observed for other Lyzl genes characterized by us in a previously [24]. Some of the Lyzl mRNA transcripts were found to be expressed only in testes in the male reproductive tract.…”

Section: Discussionmentioning

confidence: 79%

“…* -numbers indicate the position(s) of amino acid(s) in the protein. $ —The general features of LYZL proteins were reported by us earlier [24] and this table includes the previously reported data and additional analyses.…”

Section: Resultsmentioning

confidence: 99%

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In Silico and Biochemical Characterization of Lysozyme-Like Proteins in the Rat

Narmadha

Yenugu

2016

PLoS ONE

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BackgroundSpermatogenesis and sperm maturation in the male reproductive tract is dictated by a variety of proteins secreted in the testis and epididymis. Though the proteome of these tissues is known, the functional role of many of these proteins remains uncharacterized. In this study, we characterize the rat Lysozyme-like (Lyzl) genes and proteins.MethodsIn silico tools were used to predict the primary, secondary and tertiary structures. Reverse transcription PCR, immunofluorescence and immunoblotting were used to determine the expression pattern. Lysozyme like enzyme activity was assessed by standard assays.ResultsSix rat Lyzl genes namely Lyzl1, Lyzl3, Lyzl4, Lyzl5, Lyzl6 and Lyzl7 were found to be highly conserved among the vertebrates with higher homology to mouse counterparts than with human counterparts. All the LYZL proteins contained the characteristic 4 disulfide bridges similar to c-type lysozyme. Only LYZL 1 and 6, conserved the active site amino acids of the lysozyme. Molecular modeling studies indicated that LYZL proteins exhibit strikingly similar three-dimensional structures among themselves. The secondary structure analysis of the recombinant LYZL proteins indicated the presence of α-helix, β-sheet and random coil with α-helix being the majority. Docking studies indicated the peptidoglycan binding nature of LYZL proteins. All the rat Lyzl mRNA transcripts (Lyzl1, Lyzl3, Lyzl4, Lyzl5, Lyzl6 and Lyzl7) are predominantly expressed in testes though some of them are expressed in tissues other than reproductive tract. Their expression was androgen independent. The rat LYZL proteins are localized in the germinal epithelium and on the spermatozoa. Recombinant LYZL1 and 6 possessed muramidase, isopeptidase and antibacterial activities. The mechanism of antibacterial action of LYZL1 and LYZL6 involved bacterial membrane damage and leakage of cellular contents. Only LYZL1 and 6 possess peptidoglycan binding ability, whereas LYZL3, LYZL4 and LYZL5 possess hyaluronan binding ability suggesting a possible functional divergence of these proteins. LYZL3, LYZL4 and LYZL7 possessed free radical scavenging property, suggesting that they may act as antioxidants.ConclusionThe divergent properties of LYZL proteins indicate that they may have a role in sperm function, innate immunity and other physiological process as well.

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A mouse seminal vesicle‐secreted lysozyme c‐like protein modulates sperm capacitation

Lee

Lin

et al. 2021

J of Cellular Biochemistry

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Lysozyme (LYZ) c‐like proteins are primarily present in the testis and epididymis of male reproductive tissues. Here, we report a novel member of the c‐type LYZ family, the seminal vesicle‐secreted LYZ c‐like protein (SVLLP). Three forms of SVLLP were purified from mouse seminal vesicle secretions and characterized as glycoproteins with the same protein core but different N‐linked glycans. SVLLP is structurally similar to c‐type LYZ proteins. Only one of the 20 invariant residues was altered in the consensus sequence of c‐type LYZs; however, the changed residue (N53S) is one of two essential catalytic residues. LYZ activity assays demonstrated that the three glycoforms of SVLLP lacked enzyme activity. SVLLP is primarily expressed in seminal vesicles. Immunohistochemistry revealed that it occurs in the luminal fluid and mucosal epithelium of the seminal vesicles. Testosterone is not the primary regulator for its expression in the seminal vesicle. SVLLP binds to sperm and suppresses bovine serum albumin‐induced sperm capacitation, inhibits the acrosome reaction, and blocks sperm–oocyte interactions in vitro, suggesting that SVLLP is a sperm capacitation inhibitor.

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Characterization of a Novel Lysozyme-Like 4 Gene in the Rat

Cited by 15 publications

References 30 publications

Characterisation of Lyzls in mice and antibacterial properties of human LYZL6

Characterisation of Lyzls in mice and antibacterial properties of human LYZL6

In Silico and Biochemical Characterization of Lysozyme-Like Proteins in the Rat

A mouse seminal vesicle‐secreted lysozyme c‐like protein modulates sperm capacitation

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