Aspergillus niger Acid Proteinase A

Takahashi, Kenji; Kagami, Naofumi; Huang, Xiangping; Kojima, Masaki; Inoue, Hiroo

doi:10.1007/978-1-4615-5373-1_38

Cited by 14 publications

(14 citation statements)

References 19 publications

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“…Although our detecting method is not definitive, it is likely that this dust proteinase is aspergillopepsin I (aspergillopeptidase A; extracellular acid protease; proteinase B), which has been variously reported to exist as ∼22 and ∼43 kDa proteins. 28,31,32 Microbial proteinases are known to multimerize in solution and it is likely that our ∼86 kDa product represents a tetramer of aspergillopepsin I 33 (Figure 1; and P Kolattukudy personal communication). Aspergillopepsins are secreted by many aspergillus species and we have used the highly allergenic A. oryzae aspergillopepsin for many years to generate allergic lung disease in mice.…”

Section: Discussionmentioning

confidence: 99%

Link between allergic asthma and airway mucosal infection suggested by proteinase-secreting household fungi

et al. 2009

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Active fungal proteinases are powerful allergens that induce experimental allergic lung disease strongly resembling atopic asthma, but the precise relationship between proteinases and asthma remains unknown. Here, we analyzed dust collected from the homes of asthmatic children for the presence and sources of active proteinases to further explore the relationship between active proteinases, atopy, and asthma. Active proteinases were present in all houses and many were derived from fungi, especially Aspergillus niger. Proteinase-active dust extracts were alone insufficient to initiate asthma-like disease in mice, but conidia of A. niger readily established a contained airway mucosal infection, allergic lung disease, and atopy to an innocuous bystander antigen. Proteinase produced by A. niger enhanced fungal clearance from lung and was required for robust allergic disease. Interleukin 13 (IL-13) and IL-5 were required for optimal clearance of lung fungal infection and eosinophils showed potent anti-fungal activity in vitro. Thus, asthma and atopy may both represent a protective response against contained airway infection due to ubiquitous proteinase-producing fungi.

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Section: Discussionmentioning

confidence: 99%

Link between allergic asthma and airway mucosal infection suggested by proteinase-secreting household fungi

et al. 2009

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“…Bcacp1 encodes a protein of 257 amino acids sharing 89 % identity with SsACP1, 55 % identity with PrtA of Aspergillus niger (Takahashi et al, 1991) and 45 % identity with SGP of Scytalidium lignicolum (Maita et al, 1984). Despite high conservation between the sequences of SsACP1 and BcACP1, two notable differences exist.…”

Section: Isolation and Characterization Of The Bcacp1 Genementioning

confidence: 93%

pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea

et al. 2009

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During pathogenesis, the ascomycete Botrytis cinerea secretes a range of cell-wall-degrading enzymes such as polygalacturonases, glucanases and proteases. We report the identification of a new member of the G1 family of proteases, BcACP1, which is secreted by B. cinerea during infection. The production of BcACP1 correlates with the acidification of the plant tissue, and transcriptional analysis of the Bcacp1 gene showed that it is only expressed under acidic growth conditions. Using a transcriptional reporter system, we showed that pH regulation of Bcacp1 is not mediated by the canonical PacC transcription factor binding site. Like other G1 proteases, BcACP1 is produced as a pro-enzyme. Trapping of the zymogen form allowed investigation of its maturation process. Evidence is presented for an autocatalytic proteolysis of the enzyme that is triggered by acidic pH. Environmental pH therefore controls Bcacp1 production at both the transcriptional and post-translational level.

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“…Mutational data from the closely related aspergillopepsin II (A. niger carboxyl proteinase-A or AnCPA) suggested that Asp-123 and Glu-219 (mature numbering, Asp-53 and Glu-149) are the catalytic residues (20,36). The suggestion that Asp-53 (Asp-43 in SCP-B) is a catalytic residue is better interpreted as a disruption of the folding pathway of the enzyme caused by the mutation of Asp-53.…”

Section: The Binding Of Hydrolytic Products Of Angiotensin II To Scp-bmentioning

confidence: 99%

The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum

Fujinaga

Cherney

Oyama

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

100

110

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The molecular structure of the pepstatin-insensitive carboxyl peptidase from Scytalidium lignicolum, formerly known as scytalidopepsin B, was solved by multiple isomorphous replacement phasing methods and refined to an R factor of 0.230 (R free ‫؍‬ 0.246) at 2.1-Å resolution. In addition to the structure of the unbound peptidase, the structure of a product complex of cleaved angiotensin II bound in the active site of the enzyme was also determined. We propose the name scytalidocarboxyl peptidase B (SCP-B) for this enzyme. On the basis of conserved, catalytic residues identified at the active site, we suggest the name Eqolisin for the enzyme family. The previously uninvestigated SCP-B fold is that of a ␤-sandwich; each sheet has seven antiparallel strands. A tripeptide product, Ala-Ile-His, bound in the active site of SCP-B has allowed for identification of the catalytic residues and the residues in subsites S1, S2, and S3, which are important for substrate binding. The most likely hydrolytic mechanism involves nucleophilic attack of a general base (Glu-136)-activated water (OH ؊ ) on the si-face of the scissile peptide carbonylcarbon atom to form a tetrahedral intermediate. Electrophilic assistance and oxyanion stabilization is provided by the side-chain amide of Gln-53. Protonation of the leaving-group nitrogen is accomplished by the general acid function of the protonated carboxyl group of Glu-136. P epstatin-insensitive carboxyl peptidases (1-8) originally found by Murao and Oda can be classified into two groups, bacterial and fungal carboxyl peptidases. The 3D structures of the two members of the bacterial carboxyl peptidases have recently been determined (9, 10). From the tertiary folds, it was clear that these enzymes are members of the subtilisin family. Each enzyme has a glutamate residue acting as the general base instead of the histidine present in the subtilisins. The environments of the carboxylates contribute to the low pH optima of these enzymes.The fungal pepstatin-insensitive carboxyl peptidases (5) are represented by several enzymes, among them the enzyme that is the subject of this article. Formerly, this enzyme has been called Scytalidopepsin-B because of its low pH optimum and preponderance of acidic residues (8). It is isolated from Scytalidium lignicolum ATCC24568. We have chosen to rename this enzyme scytalidocarboxyl peptidase-B (SCP-B) to reflect its fungal source and active-site carboxyl groups. SCP-B is synthesized as a precursor consisting of two regions: an amino-terminal preprosegment of 54 amino acid residues and a mature enzyme consisting of 206 amino acid residues (11). The mature enzyme has no sequence similarity to the well known pepsin-like or retroviral aspartic peptidases, but it has significant similarity to the other fungal pepstatin-insensitive carboxyl peptidases (Fig. 1).SCP-B and the other carboxyl peptidases described here have been classified in family A4 of the aspartic endopeptidases in the MEROPS (http:͞͞merops.sanger.ac.uk). database. On the basis of our structur...

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Aspergillus niger Acid Proteinase A

Cited by 14 publications

References 19 publications

Link between allergic asthma and airway mucosal infection suggested by proteinase-secreting household fungi

Link between allergic asthma and airway mucosal infection suggested by proteinase-secreting household fungi

pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea

The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum

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