Cloning and characterization of the cDNAs and genes (mep20) encoding homologous metalloproteinases from Aspergillus flavus and A. fumigatus

Ramesh, M.; Sirakova, Tatiana D.; Kolattukudy, Pappachan E.

doi:10.1016/0378-1119(95)00434-8

Cited by 40 publications

(26 citation statements)

References 17 publications

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“…These include Der P I (29), the Ag most commonly linked to asthma worldwide (58), Fel d I (59), the most important allergen derived from the domestic cat and many pollens (48,60,61). Fungi are also implicated in allergic disease, and as shown in this study and elsewhere (62,63), are potent sources of active protease. Intriguingly, occupational outbreaks of asthma are associated with the handling of bacterial-derived proteases used in the manufacture of detergent products, although it is not clear from these investigations which of several bacterial products were etiologic (64,65).…”

Section: Discussionmentioning

confidence: 69%

A Protease-Activated Pathway Underlying Th Cell Type 2 Activation and Allergic Lung Disease

Kheradmand

Kiss

et al. 2002

The Journal of Immunology

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The respiratory allergens that induce experimental Th cell type 2-dependent allergic lung inflammation may be grouped into two functional classes. One class of allergens, in this study termed type I, requires priming with adjuvants remote from the lung to overcome airway tolerogenic mechanisms that ordinarily preclude allergic responses to inhaled Ags. In contrast, the other, or type II, allergen class requires neither remote priming nor additional adjuvants to overcome airway tolerance and elicit robust allergic lung disease. In this study, we show in an experimental model that diverse type II allergens share in common proteolytic activity that is both necessary and sufficient for overcoming airway tolerance and induction of pulmonary allergic disease. Inactivated protease and protease-free Ag fragments showed no allergenic potency, demonstrating that only active protease acting on endogenous substrates was essential. Furthermore, induction of airway tolerance could be aborted and allergic lung disease established by simply adding purified protease to a type I allergen. Thus, exogenous proteases are common to type II allergens and may be generally required to overcome the innate resistance of the airway to Th cell type 2 activation and allergic inflammation, raising concern for their potential contribution to diseases such as asthma.

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Section: Discussionmentioning

confidence: 69%

A Protease-Activated Pathway Underlying Th Cell Type 2 Activation and Allergic Lung Disease

Kheradmand

Kiss

et al. 2002

The Journal of Immunology

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287

292

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“…7) with the BLAST program (17). They are Aspergillus oryzae neutral protease II (accession number 1078624) (18), Aspergillus flavs 24-kDa metalloproteinase precursor (deuterolysin, accession number 1170905), Aspergillus fumigata (listed as Sartorya fumigata in protein sequence data base) MEP20, (accession number 780794) (19), and penicillolysin (accession number 1078641) from Penicillium citrinum (20). From the sequence alignment, it is apparent that they have evolved from a common ancestor, although only mushroom enzymes have the unique specificity.…”

Section: Table II Amino Acid Compositions Of Pe-pomep and Its Trypticmentioning

confidence: 99%

Amino Acid Sequences of Metalloendopeptidases Specific for Acyl-Lysine Bonds from Grifola frondosa and Pleurotus ostreatus Fruiting Bodies

Nonaka

Dohmae

Hashimoto

et al. 1997

Journal of Biological Chemistry

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The complete amino acid sequences of two lysine-specific zinc metalloendopeptidases (EC 3.4.24), Grifola frondosa metalloendopeptidase (GFMEP) and Pleurotus ostreatus metalloendopeptidase (POMEP), from the fruiting bodies of these two edible mushrooms have been established based on the sequence information of the peptides generated from the reduced and alkylated GFMEP and POMEP by proteolytic digestions using GFMEP, trypsin, and other proteinases as well as by several chemical cleavages. From the sequences, it was found that GFMEP and POMEP were polypeptides composed of 167 and 168 amino acid residues, from which their molecular weights were calculated to be 18,040. Comparison of the sequences revealed that overall identity between the enzymes was 61.3%. Although a highly homologous sequence was not found in sequence data bases except for a consensus zinc-binding sequence, HEXXH, both metalloendopeptidases somewhat resembled a family of metalloproteinases categorized as deuterolysin. These proteases together with GFMEP and POMEP do not have conserved third and/or fourth liganding amino acid residues seen in metzincin or thermolysin superfamily proteins and belong to a novel zinc metalloendopeptidase superfamily.

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“…In the 3Ј-UTR, we could not find the consensus sequences of polyadenylation signal but a similar sequence, AATATA, was found about 30 nucleotides upstream of the poly(A) site. Since polyadenylation signals of yeast and fungus are known to be less conserved (De Groot et al, 1996;Humphrey and Proudfoot, 1988;Penas et al, 1998;Ramesh et al, 1995;Zhao et al, 1999), it is quite possible that the AATATA sequence functions as the polyadenylation signal.…”

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confidence: 99%

“…The amino acid sequence of GfMEP was aligned with other aspzincins, AmMEP (EMBL AJ238718), MEP from Aeromonas hydrophila (AhMEP) (Chang et al, 1997), penicillolysin (Matsumoto et al, 1994), MEPs from Aspergillus orysae (NPII) (Tatsumi et al, 1991), A. flavus (AflMEP) (Ramesh et al, 1995), and A. fumigatus (AfuMEP) (Ramesh et al, 1995) (Fig. 2A).…”

mentioning

confidence: 99%

PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa.

Saito

Dohmae

Tsujimoto

et al. 2002

J. Gen. Appl. Microbiol.

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Metalloendopeptidases (MEPs) are widely distributed from bacteria to mammals, and they carry out various important roles. Many MEPs have been classified into two major families, "gluzincins" and "metzincins," according to the structural topology around the active site (Bode et al., 1993;Hooper, 1994;Rawlings and Barrett, 1995). We have purified and characterized uniquely specific peptidyl-Lys MEPs from edible mushrooms, Grifola frondosa (GfMEP) (Nonaka et al

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Cloning and characterization of the cDNAs and genes (mep20) encoding homologous metalloproteinases from Aspergillus flavus and A. fumigatus

Cited by 40 publications

References 17 publications

A Protease-Activated Pathway Underlying Th Cell Type 2 Activation and Allergic Lung Disease

A Protease-Activated Pathway Underlying Th Cell Type 2 Activation and Allergic Lung Disease

Amino Acid Sequences of Metalloendopeptidases Specific for Acyl-Lysine Bonds from Grifola frondosa and Pleurotus ostreatus Fruiting Bodies

PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa.

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