Investigation into white spots in the carapace of a moribund mud crab (Scylla serrata) from a white spot syndrome virus (WSSV) positive zone in Moreton Bay, Australia.

Background: A freshly deceased mud crab (Scylla serrata) exhibiting multiple white spots under the carapace was found in Pumicestone Passage, northern Moreton Bay in May 2018. This crab was taken from within a biosecurity zone established due to a recent incursion of White Spot Syndrome Virus (WSSV) into populations of wild penaeids (Penaeus spp., Metapenaeus spp.

Differential effects of zinc and magnesium ions on mineralization activity of phosphatidylserine calcium phosphate complexes.

Mg(2+) and Zn(2+) are present in the mineral of matrix vesicles (MVs) and biological apatites, and are known to influence the onset and progression of mineral formation by amorphous calcium phosphate (ACP) and hydroxyapatite (HAP). However, neither has been studied systematically for its effect on mineral formation by phosphatidylserine-Ca(2+)-Pi complexes (PS-CPLX), an important constituent of the MV nucleation core. Presented here are studies on the effects of increasing levels of Mg(2+) and Zn(2+) on the process of mineral formation, either when present in synthetic cartilage lymph (SCL), or when incorporated during the formation of PS-CPLX.

Mineralization of annexin-5-containing lipid-calcium-phosphate complexes: modulation by varying lipid composition and incubation with cartilage collagens.

Matrix vesicles (MVs) in the growth plate bind to cartilage collagens and initiate mineralization of the extracellular matrix. Native MVs have been shown to contain a nucleational core responsible for mineral formation that is comprised of Mg(2+)-containing amorphous calcium phosphate and lipid-calcium-phosphate complexes (CPLXs) and the lipid-dependent Ca(2+)-binding proteins, especially annexin-5 (Anx-5), which greatly enhances mineral formation. Incorporation of non-Ca(2+)-binding MV lipids impedes mineral formation by phosphatidylserine (PS)-CPLX.

Analysis and molecular modeling of the formation, structure, and activity of the phosphatidylserine-calcium-phosphate complex associated with biomineralization.

The nucleational core of matrix vesicles contains a complex (CPLX) of phosphatidylserine (PS), Ca(2+), and inorganic phosphate (P(i)) that is important to both normal and pathological calcification. Factors required for PS-CPLX formation and nucleational activity were studied using in vitro model systems and molecular dynamic simulations. Ca(2+) levels required for and rates of PS-CPLX formation were monitored by light scattering at 340 nm, assessing changes in amount and particle size.