Shrimp single WAP domain (SWD)-containing protein exhibits proteinase inhibitory and antimicrobial activities

Amparyup, Piti; Donpudsa, Suchao; Tassanakajon, Anchalee

doi:10.1016/j.dci.2008.06.005

Cited by 87 publications

(55 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The pellets were resuspended in 20 mM Tris-HCl (pH 8.0) and disrupted by an ultrasonic oscillator. The rSP-PmPPAE2 and rWSSV453, as a thioredoxin (trx) fusion protein (rWSSV453-trx), were each purified and refolded as described previously (35). In addition, the WSSV453 PCR product was digested with EcoRI and XhoI and cloned into the EcoRI/XhoI sites of the pET43.1a expression vector (Novagen) containing the NUS fusion protein.…”

Section: Cloning and Recombinant Protein Expression Of Pmppae2mentioning

confidence: 99%

Suppression of Shrimp Melanization during White Spot Syndrome Virus Infection

Sutthangkul

Amparyup

Charoensapsri

et al. 2015

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background: Melanization plays a major role in invertebrate defense. Results: Suppression of shrimp melanization increased the WSSV susceptibility. The viral protein, WSSV453, interferes the proPO system via PmPPAE2 inhibition. Conclusion: Shrimp melanization has an antiviral role. WSSV overcomes this by suppressing the host proPO proteinase cascade. Significance: The regulation of shrimp melanization during WSSV infection was first demonstrated.

show abstract

Section: Cloning and Recombinant Protein Expression Of Pmppae2mentioning

confidence: 99%

Suppression of Shrimp Melanization during White Spot Syndrome Virus Infection

Sutthangkul

Amparyup

Charoensapsri

et al. 2015

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…Similarly, crustin, a cystein-rich peptide that contains a whey acidic protein (WAP) domain also has antibacterial activity against Gram-positive bacteria, but some type II and III crustins have the ability to respond to both Gram-positive and negative bacteria (Donpudsa et al, 2010b). Type III crustins may also have proteinase inhibitory activities (Amparyup et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Investigation of an Idiopathic Lesion in Redclaw Crayfish Cherax Quadricarinatus Using Suppression Subtractive Hybridization

Rusaini¹,

Ariel²,

Burgess³

et al. 2013

JVM

View full text Add to dashboard Cite

Lesions indicative of putative parvovirus infection were detected in a population of freshwater redclaw crayfish (Cherax quadricarinatus) displaying hypertrophied nuclei, while these changes were undetected in another population. These changes were characterised by hypertrophic nuclei with marginated chromatin but without Cowdry type A (CA) intranuclear inclusion bodies. Suppression subtractive hybridization (SSH) was performed to generate a cDNA forward library between the two populations of crayfish. A total of 323 sequences were analysed from SSH libraries. These sequences were grouped into 76 consensus sequences and clustered into 8 categories based on sequence homology from the NCBI GenBank database. Even though histopathological observations consistently revealed lesions presumptive of putative parvovirus in C. quadricarinatus as previously reported, the molecular method failed to confirm a viral aetiology. Despite the absence of viral gene detection and therefore a conclusion of an idiopathic aetiology, the health status of these two populations of redclaw crayfish was different, resulting in differentially expressed immune-related genes in the two populations, with some genes being up-regulated in the hypertrophied nuclei population. Furthermore, the absence of parvovirus from the SSH libraries indicates that perhaps the viral messenger RNA was in too low a concentration to be detected or does not have any poly(A) tail which the SSH methodology needs to function correctly.

show abstract

“…The apolipoproteins are high molecular mass polypeptides. The LPI generally contains a fewer number of apoproteins or subunits than the LPII or Vg [28] .…”

Section: Lipoproteinmentioning

confidence: 99%