FIGURE 11.4 Structure of 2-palmitoyl-3-hydroxyphthioceranoyl-2/-sulfate-a — a'-D-trealose (Ac2SGL).


and consists of two distinguishable protein subunits, which contain at least three covalently attached bilin chromophores, open chain tetrapyrroles with no metal complexes.41 The antiviral mechanism for this alga-protein remains to be elucidated, but it has shown to abate the apoptotic activity in enterovirus 71-infected cells. It is known that enterovirus 71 infection induces apoptosis and apoptosis may help to spread viral progeny, but also contribute to the viral-induced pathology, especially if it occurs in nonreplicating cells such as neurons. During the last outbreak of enterovirus 71 infection in Taiwan, the postmortem studies clearly showed that enterovirus 71 infected the central nervous system, therefore it can be speculated that a molecule like the allophycocianin could be very helpful to reduce the severe consequences associated with the enterovirus 71 Infection.18 Allophycocianin could also be useful as a therapeutic treatment for other diseases in which the apoptotic activity is increased and related to the pathology of the disease.

Carbohydrate-Binding Proteins (CBP)

An antiviral protein with molecular weight of 29 kDa has been identified from S plantensis.22 This protein belongs to the group of carbohydrate-binding proteins (CBP) which have been found in many species including cyanobacteria, sea corals, alga, plants, invertebrates, and vertebrates. CBPs have shown a potent anti-HIV activity, presumably acting by direct binding to the glycans that are abundantly present on the HIV-1 gP120 envelope. The cyanovirin (CV-N) protein is a CBPisolated from the cyanobacteria Nostoc ellipsosporum. It is an antiviral 11-kDa protein, which has been successfully expressed as a recombinant protein in Streptococcus gordonii. This bacteria produces two forms of the CV-N, one is attached to the bacterial surface and the other, is secreted in soluble form in the supernatant of liquid bacterial cultures. The secreted form of CV-N can tightly bind to HIV-1 gp120, whereas CV-N displayed on the bacterial cell wall surface is able to efficiently capture HIV virions. Also, it has been expressed in Lactobacillus jensenii.23 These bacterial systems could be very useful to express and delivery these antiviral proteins in mucosal tissues, and protect the sites from infection of viruses like HV-1, which are highly inhibited by this type of proteins.23

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