Cloning of human lysozyme gene and expression in the yeast Saccharomyces cerevisiae

Castañón, Maria J.; Spevak, W; Gr, Adolf; Chlebowicz-Sledziewska, Ewa; Sledziewski, A

doi:10.1016/0378-1119(88)90359-9

Cited by 41 publications

(11 citation statements)

References 39 publications

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“…Since no dena turing steps were carried out during the isolation of the re combinant protein, we anticipate that if any potential en zymatic activity was present, it should have been retained. Furthermore, different kinds of lysozymes expressed in S. cerevisiae were shown to be enzymatically active [9,10].…”

Section: Discussionmentioning

confidence: 99%

Lack of Lysozyme Activity of Natural and Yeast-Derived Recombinant Der p 2

Hakkaart

Aalberse²,

Ree³

1997

Int Arch Allergy Immunol

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For Dermatophagoides pteronyssinus a number of allergens have been reported. Although the function of several allergens is known, that of the house dust mite allergen Der p 2 is unknown. A role as lysozyme has been suggested. We tested a yeast-derived recombinant Der p 2 for its lysozymatic activity. This recombinant allergen and affinity-purified natural Derp2 lacked this enzymatic activity. Whole-body mite extract retained its lysozymatic activity after removal of the group 2 allergen by monoclonal antibody depletion. Analysis of spent medium revealed the reciprocal: it contained group 2 allergen, but lacked lysozymatic activity. Together, these data demonstrate that mite lysozyme and Der p 2 are different components of mite extract.

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Section: Discussionmentioning

confidence: 99%

Lack of Lysozyme Activity of Natural and Yeast-Derived Recombinant Der p 2

Hakkaart

Aalberse²,

Ree³

1997

Int Arch Allergy Immunol

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“…The final constructs were derived from the partial human lysozyme cDNA clone HL-1421 (Castanon et aL, 1988). Bovine [5-casein regulatory elements were obtained from genomic clones pH 9.3, containing 9.0 kb of 5'-flanking DNA and the coding regions (through exon 7), and pH 4.5 consisting of the rest of the [3-casein genomic DNA including nontranslated exon 9 and 3.5 kb of 3' flanking DNA (Gorodestsky et aL, 1988).…”

Section: Dna Constructsmentioning

confidence: 99%

Expression of human lysozyme mRNA in the mammary gland of transgenic mice

Maga

Anderson

Huang

et al. 1994

Transgenic Research

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Owing to its inherent antimicrobial effect and positive charge, the expression of human lysozyme in bovine milk could be beneficial by altering the overall microbial level and the functional and physical properties of the milk. We have used transgenic mice as model systems to evaluate the expression of human lysozyme containing fusion gene constructs in the mammary gland. Expression of human lysozyme was targeted to the mammary gland by using the 5' promoter elements of either the bovine beta (line B mice) or alpha s1 (line H mice) casein genes coupled to the cDNA for human lysozyme. Expression of human lysozyme mRNA was not found in mammary tissue from any of line B mice. Tissues were analysed from six lines of H mice and two, H6 and H5, were found to express human lysozyme mRNA in the mammary gland at 42% and 116%, respectively, of the levels of the endogenous mouse whey acidic protein gene. At peak lactation, female mice homozygous for the H5 and H6 transgene have approximately twice the amount of mRNA encoding human lysozyme as hemizygous animals. Expression levels of human lysozyme mRNA in the mammary gland at time points representing late pregnancy, early, peak and late lactation corresponded to the profile of casein gene expression. Human lysozyme mRNA expression was not observed in transgenic males, virgin females or in the kidney, liver, spleen or brain of lactating females. A very low level of expression of human lysozyme mRNA was observed in the salivary gland of line H5.

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“…The regulation of the chicken lysozyme gene has been studied in the most detail (Elgin 1988(Elgin , 1990Stief et al 1989;Bonifer et al 1990;Phi-Van et al 1990). Though characterized to a lesser extent, lysozyme genes from other vertebrates, specifically mammals, have been isolated (Castafi6n et al 1988;Chung et al 1988;Cross et al 1988;Yoshimura et al 1988;Peters et al 1989;Cross and Renkawitz 1990;Cortopassi and Wilson 1990;Swanson et al 1991). The human genome contains a single lysozyme gene (Peters et al 1989).…”

Section: Introductionmentioning

confidence: 99%

Characterization of the cow stomach lysozyme genes: Repetitive DNA and concerted evolution

1993

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Cow stomach lysozyme genes have evolved in a mosaic pattern. The majority of the intronic and flanking sequences show an amount of sequence difference consistent with divergent evolution since duplication of the genes 40-50 million years ago. In contrast, exons 1, 2, and 4 and immediately adjacent intronic sequences differ little between genes and show evidence of recent concerted evolution. Exon 3 appears to be evolving divergently. The three characterized genes vary from 5.6 to 7.9 kilobases in length. Different distributions of repetitive DNA are found in each gene, which accounts for the majority of length differences between genes. The different distributions of repetitive DNA in each gene suggest the repetitive elements were inserted into each gene after the duplications that give rise to these three genes and provide additional support for divergent evolution for the majority of each gene. The observation that intronic and flanking sequences are evolving divergently suggests that the concerted evolution events involved in homogenizing the coding regions of lysozyme genes involve only one exon at a time. This model of concerted evolution would allow the shuffling of exon-sized pieces of information between genes, a phenomenon that may have aided in the early adaptive evolution of stomach lysozyme.

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Cloning of human lysozyme gene and expression in the yeast Saccharomyces cerevisiae

Cited by 41 publications

References 39 publications

Lack of Lysozyme Activity of Natural and Yeast-Derived Recombinant Der p 2

Lack of Lysozyme Activity of Natural and Yeast-Derived Recombinant Der p 2

Expression of human lysozyme mRNA in the mammary gland of transgenic mice

Characterization of the cow stomach lysozyme genes: Repetitive DNA and concerted evolution

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