Moreover, small chemical compounds fostering aggregation of VP26 might be developed into effective 
antiviral therapy that prevents HSV nuclear capsid egress and thus virion formation. On the other hand, for characterization of intracellular capsid trafficking, virion assembly and cell entry, we will base future tagging or disabling mutations in HSV1 proteins on HSV1 that has a low propensity for nuclear aggregation, and therefore seems to contain a less invasive tag on VP26. Furthermore, its subcellular capsid distribution during the course of an infection resembles more that of untagged capsids when compared to the other tags on VP26. Her-2, Estrogen Mepiroxol receptor and Progesterone Receptor are the most commonly used biomarkers and therapeutic targets in breast cancer patients. However, these biomarkers are not expressed in 17�C30% of women with breast cancer which limits the use of existing therapies. Patients under hormone deprivation and Herceptin therapy, a most common therapeutic option, tend to acquire resistance to such therapies over time. Whereas, the triple negative breast cancer phenotype, which lacks the presence of Her-2, ER and PR are even more aggressive and resistant. Therefore there is an urgent clinical need to identify new diagnostic as well as therapeutic markers for early diagnosis and treatment of such patients. Herceptin, like other humanized receptor targeted monoclonal antibodies, inhibits the growth and progression in Her-2 positive breast tumors by blockade of downstream survival pathway. However, recent reports suggest that cells acquire resistance to the targeted therapies against receptor tyrosine kinases by several mechanisms. One of the most commonly seen mechanism is the activation of other receptor RTKs such as EGFR, IGFR and non-receptor tyrosine kinases such Src. The overexpression of EGFR and Src in both Her-2 negative and TNBC cells contributes significantly to the tumor growth and progression. Considering the heterogeneity of cancer cells, it is predicted that not only these RTKs, but also other proteins which are required for normal functioning of these proteins are also upregulated in such cells. We found that Annexin A2, a calcium dependent phospholipid binding protein, is inversely correlated with Her-2 expression. This observation holds true in case of Herceptin resistance, both in experimental and clinical situations. AnxA2 is aberrantly expressed in various human cancers. It is present as a monomer in the nucleus, but as a heterotetramer with p11 in the cytosol to bind to the inner and outer leaflets of the plasma membrane. The cytosolic AnxA2 is mobilized to the cell Atropine sulfate surface upon phosphorylation at the Nterminal Serine 25 and Tyrosine 23, by different kinases such as PKC and Src as well as treatment with calcium ionophore or calcium inducing agents such as glutamate. The cell surface associated AnxA2 heterotetramer, is a receptor for both plasminogen and tissue type plasminogen activator and acts as a catalytic center for the activation of plasminogen to plasmin which helps in invasion and metastasis of cancer cells. The membrane associated AnxA2 interacts with RTKs such as like insulin receptor, insulin-like growth factor receptor and non-receptor tyrosine kinases such as focal adhesion kinase and Src. AnxA2 acts as a key scaffolding protein in anchoring and transportation of several proteins within plasma membrane as well as from cytosol to the plasma membrane, and contributes to cell signaling, angiogenesis and matrix degeneration. Our recent data show that stimulation of AnxA2 by calcium ionophore or a phosphomimetic mutant of AnxA2 leads to its localization to the lipid raft component of the cell membrane, where it interact with different proteins and also leads to its own exosomal association.