One of the drawbacks of currently available inactivated vaccines is the lack of broad cross-protective humoral and cell-mediated immune response against any influenza virus. Their efficacy is limited due to the genetic variation of influenza viruses. Therefore, their annual reformulation is necessary in an attempt to antigenically match the currently circulating strain for each of the three vaccine strains or their subunits (HA and NA of H1N1 and H3N2 of influenza A virus as well as of influenza B virus) from which they are composed. Increasing amount of information about conserved epitopes of influenza viruses brings us closer to the development of the universal vaccine. Such vaccine should contain both, conserved B-cell epitopes that are important for induction of cross-protective antibodies and CTL epitopes for the involvement of the cellular arm of the immune response to the overall protective effect [90] . It was shown that the pre-existing memory T-cell immunity as defense against seasonal influenza strains may have the capacity to moderate the course of disease in the case of newly emerging flu viruses in the absence of cross-reactive antibody response [86, 93, 123, 124] . It was also shown that it would be possible to elicit the CTL response simultaneously directed against multiple supertype-restricted conserved CTL epitopes [135] [136] [137] [138] [139] . This could be relevant for the development of a potential supertype-restricted multiepitope CTL based vaccine, with the effort to reach wide population coverage. Even though recent reports support a beneficial role of T-cell response in reducing human infections [86] [87] [88] 124] , there are still many questions regarding the feasibility of designing an effective supertype-restricted CTL epitope based vaccine in humans. In addition to CTL epitopes, B-cell epitopes from conserved influenza antigens that can elicit cross-protective humoral response should also be considered as a component of novel vaccines. Recently, highly cross-reactive monoclonal antibodies directed against conserved epitopes of HA2 subunit, including fusion peptide, were identified [28, 30, 66, [68] [69] [70] . HA2 subunit region as well as M2 protein are promising candidates for design of vaccine constructs aimed at providing broad-spectrum immunity to influenza viruses [1, 28, 31, 37, 45] . Cross-protective potential of HA2 and eM2 could be increased by optimization of their delivery and immunogenicity using vaccine vectors that target multiple Toll-like receptors for efficient stimulation of innate immunity and subsequent enhancement of the adaptive immune response [41, 140] . Conserved B-and T-cell epitopes, thus, could represent the basis for preparation of universal vaccine and bring new hope for development of pandemic or universal influenza vaccine.  The intracellular dynamic of protein palmitoylation S-palmitoylation describes the reversible attachment of fatty acids (predominantly palmitate) onto cysteine residues via a labile thioester bond. This posttranslational modification impacts protein functionality by regulating membrane interactions, intracellular sorting, stability, and membrane micropatterning. Several recent findings have provided a tantalizing insight into the regulation and spatiotemporal dynamics of protein palmitoylation. In mammalian cells, the Golgi has emerged as a possible super-reaction center for the palmitoylation of peripheral membrane proteins, whereas palmitoylation reactions on post-Golgi compartments contribute to the regulation of specific substrates. In addition to palmitoylating and depalmitoylating enzymes, intracellular palmitoylation dynamics may also be controlled through interplay with distinct posttranslational modifications, such as phosphorylation and nitrosylation. Cellular proteins undergo a vast array of dynamic and static modifications to their amino acid backbone, which can dramatically extend and regulate functional output. Some of these modifications, phosphorylation in particular, have been the subject of intensive research, and their regulation and intracellular functions are extensively characterized. In contrast, our understanding of S-palmitoylation (hereafter referred to as palmitoylation), the attachment of palmitate (C16:0) or other long chain fatty acids to cysteine residues, has lagged behind some of its more popular cousins. Indeed, enzymes that catalyze palmitoylation reactions have only recently been identified after landmark studies in yeast, settling a long-running debate as to whether this process was predominantly enzyme mediated or spontaneous (Lobo et al., 2002; Roth et al., 2002; Fukata et al., 2004; Keller et al., 2004) .