Our results share similarities with the findings of studies investigating interactions among chaperones and other Afatinib EGFR/HER2 inhibitor proteins in the model yeast S. cereviseae. For example, both fungi demonstrated interactions of Hsp60 with chaperonins Hsp82, Ssa4 and Sse1. Furthermore, other well characterized interactions in S. cereviseae were observed in Hc at elevated temperatures, such as with proteins involved in carbohydrate metabolism and protein metabolism. We conclude that Hc Hsp60 is a key regulator of diverse cellular processes, including amino acid, protein, lipid, and carbohydrate metabolism, cell signaling, replication, and expression of virulence associated proteins. Hsp60 apparently contributes with cell wall changes that allow the pathogen to survive under stress conditions. In addition, these data open a new perspective since these interactions could potentially modify the way that host immune cells recognize the pathogen possibly modulating the immune response. Due to the high homology of Hsp60 proteins in different organisms, the fact that Hsp60 is secreted by Hc, and our present demonstration of the promiscuity of Hc Hsp60, this protein could also act as a scavenger of host proteins and thus modify host immune responses. The broad interaction capacity of Hsp60 opens numerous interesting avenues for future study, including drug targeting and immunoterapy for treating lifethreatening fungal infections. Wild aquatic birds, such as Anseriformes and Charadriiformes are reservoir hosts for avian influenza viruses. However, AIVs can cause outbreaks in poultry. In some instances, AIV strains from poultry hosts have increased pathogenicity for poultry species, and have acquired an ability to WZ4002 EGFR/HER2 inhibitor infect mammalian hosts, and/or have caused fatal infections in humans. Therefore, to minimize adverse effects in humans and poultry from AIV infections, it is important to understand what evolutionary changes occur in AIVs when they are transmitted from wild birds to poultry. Understanding these evolutionary changes can lead to better detection, prevention and control strategies. AIVs interact with their hosts mostly through two glycoproteins, Hemagglutinin and Neuraminidase. HA recognizes receptors on target cells and NA, a sialidase, assists virus entry and release. One observation that has been reported in viruses isolated during separate poultry outbreaks is a deletion in the stalk region of the NA. The stalk is a structure that separates the enzymatically and antigenically active ����head���� from the hydrophobic domain embedded in the viral membrane. Little is known about the biological function of the NA stalk.