Proteolytic activities in body and faecal extracts of the storage mite, Acarus farris

Sánchez‐Ramos, Ismael; Hernández, Carlos Martínez; Castañera, Pedro; Ortego, Félix

doi:10.1111/j.0269-283x.2004.00518.x

Cited by 25 publications

(18 citation statements)

References 40 publications

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“…Legend: Ã denotes a significant difference from the control based on Tukey's post-hoc comparison at P 5 0.05. explanation because it decreased general proteolytic activity on azocasein. A similar situation was observed in previous studies (Montealegre et al, 2002;Sanchez-Ramos et al, 2004). This event may be interpreted as such: increased cysteine protease activity in mite homogenates does not compensate for the decrease in general proteolytic activity caused by the disruption of disulfide bridges within other proteases, which may inactivate them (Marianayagam et al, 2004).…”

Section: Discussionsupporting

confidence: 83%

“…The enzymatic activities of the small peaks at pH 3 suggest the presence of aspartate proteases. Aspartate protease activity has previously been found in A. farris (Sanchez-Ramos et al, 2004), A. siro (Nisbet and Billingsley, 2000), and T. putrescentiae (Ortego et al, 2000). The authors in these previous studies suggested that aspartate proteases in acaridid mites are non-digestive.…”

Section: Discussionmentioning

confidence: 91%

“…The enzymatic and inhibitory assays confirmed the presence of serine, cysteine, and aspartate proteases in the stored-product mite, Acarus farris (Sanchez-Ramos et al, 2004). Proteases were analyzed in another stored-product mite, Acarus siro, and the predator mite, Cheyletus malaccensis, to a lesser extent .…”

mentioning

confidence: 76%

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Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites

Erban

Hubert

2010

Arch Insect Biochem Physiol

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Microplate assays with 96 wells were optimized to screen proteolytic activities in mite homogenates. Whole-mite extracts of Acarus siro, Aleuroglyphus ovatus, Tyrophagus putrescentiae, Tyroborus lini, Carpoglyphus lactis, Lepidoglyphus destructor, and Dermatophagoides farinae exhibited non-specific proteolytic activity in buffers from pH 2 to 12, and three peaks of highest activity at pH 3, 5-6, and 10 were distinguished. The reducing agent Tris(2-carboxyethyl)phosphine hydrochloride decreased general proteolytic activity on azocasein at pH 5 and 6. The results obtained on two non-specific substrates, azocasein and azoalbumin, showed highly different ranks of the species at pH 5 and 6. Proteolytic activities toward N(α)-Benzoyl-D,L-arginine 4-nitroanilide hydrochloride, N-Succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine 4-nitroanilide, N-Succinyl-L-alanyl-L-alanyl-L-alanine 4-nitroanilide, Benzyloxycarbonyl-L-arginine-L-arginyl 4-nitroanilide, and N-Methoxysuccinyl-L-alanyl-L-alanyl-L-prolyl-L-methionine 4-nitroanilide (MAAPMpNA) were highest at alkaline pH, but the activity toward MAAPMpNA was also high at pH 5 and 6. In contrast, N-Succinyl-L-alanyl-L-alanyl-L-phenylalanine 4-nitroanilide (AAPpNA) and L-arginyl 4-nitroanilide (ArgpNA) had the highest activity recorded at pH 6. The high activities observed on AAPpNA, ArgpNA, and MAAPMpNA at digestive pH suggest that enzymes present in these extracts could have the majority of proteolysis in the mite gut. Evidence of the presence of proteolytic activities on all tested substrates and in all the tested mite homogenates suggests that the proteolytic activities may contribute to allergenicity. Poor or undetected hydrolytic activities of mite extracts toward substrates for keratin and collagen at digestive pH underline the importance of ecological interactions between mites and microorganisms in the utilization of such substrates.

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Section: Discussionsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 91%

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Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites

Erban

Hubert

2010

Arch Insect Biochem Physiol

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“…Some of them with enzymatic activity included groups 1, 3, 4, 6, 8, 9 and 15 [4, 5]. Other mite species, such as Glycyphagus domesticus [6], Acarus farris [7], Tyrophagus putrescentiae [8], Blomia tropicalis [9, 10], Psoroptes cuniculi [11] and Aleuroglyphus ovatus [12] also contain allergens with enzymatic activity. Serine proteases (trypsin and chymotrypsin) seem to be more abundant in faecal than in whole body extracts [13, 14].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Activity of Dermatophagoides pteronyssinus Extracts after Acidic Treatment

Fernández-Caldas¹,

Gallego²,

Carnés³

et al. 2007

Int Arch Allergy Immunol

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Background: Mite extracts contain potent enzymes. These enzymes, especially Der p 1, may affect the bronchial homeostasis and the amplification of the allergic response. The objectives of this study were to determine how depigmentation affects the enzymatic activity of allergen extracts of Dermatophagoides pteronyssinus and to verify if these depigmented extracts retain their in vitro allergenic properties. Methods: Four native extracts were manufactured from 4 different batches of raw material of D. pteronyssinus. Once extracted, native extracts were reconstituted and modified by adding increasing quantities of 2 M HCl to the solution and dialyzed against double-distilled water. The enzymatic activity of these 8 extracts (4 native and 4 depigmented) was evaluated using in vitro methods. The allergenic potency was evaluated by human specific IgE and IgG ELISA inhibition experiments. The major allergen content (Der p 1 and Der p 2) was measured with monoclonal antibodies. Results: Protease, phosphatase, lipase and glycosidase activity was detected in native extracts. After depigmentation, all the enzymatic activities showed a significant decrease. SDS-PAGE reveals the same protein profile in both types of extracts. The results of ELISA inhibition confirmed that depigmented extracts preserved their antigenic and allergenic capacity. Der p 2 levels increased in depigmented extracts, while the detection capacity of Der p 1 decreased. Conclusions: The depigmentation process significantly reduced the enzymatic activity of these mite extracts, while preserving their allergenicity and antigenicity. No significant differences were observed in the antigenic profile of native and depigmented extracts.

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“…Other mite species, e.g. Glycyphagus domesticus [9], Acarus farris [10], Tyrophagus putrescentiae [11], Blomia tropicalis [12,13,14], Psoroptes cuniculi [15] and Aleuroglyphus ovatus [16],also contain potent enzymes. Comparative studies have been conducted to analyze the presence of enzymes in mite bodies and spent media.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Activity in Body and Fecal Extracts of the Storage Mite Chortoglyphus arcuatus

Carnés¹,

Boquete

Carballada

et al. 2007

Int Arch Allergy Immunol

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Background:Chortoglyphus arcuatus has been described in many countries. Many allergens are potent enzymes, which may promote a Th2 immune response. The aim of this study was to evaluate the enzymatic activity of body and fecal extracts of C. arcuatus. Material and Methods: Feces and bodies of full-grown C. arcuatus cultures were separated by sieving, extracted in PBS, dialyzed and lyophilized. The antigenic profile of both extracts was determined by SDS-PAGE. Immunoblot experiments were conducted using a pool of sera from allergic individuals residing in Galicia, a region of Spain, where this species is abundant. The enzymatic activity of the extracts was evaluated by the zymogram technique. Serine and cysteine protease activity was measured using in vitro methods. The API Zym® system was used to determine the enzymatic properties of the extracts. Results: The antigenic profile showed that the body extract contained more and better defined bands than the fecal extract. Allergens were detected in both extracts in a molecular weight range between 14 and 100 kDa. Gelatinolytic gels confirmed that fecal extracts contain more hydrolytic enzymatic activity than body extracts. Serine protease activity in fecal extracts was higher than in body extracts (5.98 vs. 2.701 IU of trypsin/mg of freeze-dried material). No cysteine protease activity was detected. Conclusion:C. arcuatus extracts contain several allergens and proteins with high enzymatic activity, especially in the feces. Some of these allergens may be enzymes. Fecal extracts have more enzymatic activity than body extracts.

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Proteolytic activities in body and faecal extracts of the storage mite, Acarus farris

Cited by 25 publications

References 40 publications

Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites

Comparative analyses of proteolytic activities in seven species of synanthropic acaridid mites

Enzymatic Activity of <i>Dermatophagoides pteronyssinus</i> Extracts after Acidic Treatment

Enzymatic Activity in Body and Fecal Extracts of the Storage Mite <i>Chortoglyphus arcuatus</i>

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