Bacteriophages are specific antagonists to bacterial hosts. These viral entities have attracted growing interest as optimal vaccine delivery vehicles. Phages are well-matched for vaccine design due to being highly stable under harsh environmental conditions, simple and inexpensive large scale production, and potent adjuvant capacities. Phage vaccines have efficient immunostimulatory effects and present a high safety profile because these viruses have made a constant relationship with the mammalian body during a long-standing evolutionary period. The birth of phage display technology has been a turning point in the development of phage-based vaccines. Phage display vaccines are made by expressing multiple copies of an antigen on the surface of immunogenic phage particles, thereby eliciting a powerful and effective immune response. Also, the ability to produce combinatorial peptide libraries with a highly diverse pool of randomized ligands has transformed phage display into a straightforward, versatile and high throughput screening methodology for the identification of potential vaccine candidates against different diseases in particular microbial infections. These libraries can be conveniently screened through an affinity selection-based strategy called biopanning against a wide variety of targets for the selection of mimotopes with high antigenicity and immunogenicity. Also, they can be panned against the antiserum of convalescent individuals to recognize novel peptidomimetics of pathogen-related epitopes. Phage display has represented enormous promise for finding new strategies of vaccine discovery and production and current breakthroughs promise a brilliant future for the development of different phage-based vaccine platforms.

No abstract

No abstract

No abstract

Fc-fusion proteins are composed of Fc region of IgG antibody (Hinge-CH2-CH3) and a desired linked protein. Fc region of Fc-fusion proteins can bind to neonatal Fc receptor (FcRn) thereby rescuing it from degradation. The first therapeutic Fc-fusion protein was introduced for the treatment of AIDS. The molecular designing is the first stage in production of Fc-fusion proteins. The amino acid residues in the Fc region and linked protein are very important in the bioactivity and affinity of the fusion proteins. Although, therapeutic monoclonal antibodies are the top selling biologics but the application of therapeutic Fc-fusion proteins in clinic is in progress and among these medications Etanercept is the most effective in therapy. At present, eleven Fc-fusion proteins have been approved by FDA. There are novel Fc-fusion proteins which are in pre-clinical and clinical development. In this article, we review the molecular and biological characteristics of Fc-fusion proteins and then further discuss the features of novel therapeutic Fc-fusion proteins.

Over the recent decades, the use of antibody-drug conjugates (ADCs) has led to a paradigm shift in cancer chemotherapy. Antibody-based treatment of various human tumors has presented dramatic efficacy and is now one of the most promising strategies used for targeted therapy of patients with a variety of malignancies, including hematological cancers and solid tumors. Monoclonal antibodies (mAbs) are able to selectively deliver cytotoxic drugs to tumor cells, which express specific antigens on their surface, and has been suggested as a novel category of agents for use in the development of anticancer targeted therapies. In contrast to conventional treatments that cause damage to healthy tissues, ADCs use mAbs to specifically attach to antigens on the surface of target cells and deliver their cytotoxic payloads. The therapeutic success of future ADCs depends on closely choosing the target antigen, increasing the potency of the cytotoxic cargo, improving the properties of the linker, and reducing drug resistance. If appropriate solutions are presented to address these issues, ADCs will play a more important role in the development of targeted therapeutics against cancer in the next years. We review the design of ADCs, and focus on how ADCs can be exploited to overcome multiple drug resistance (MDR).

Phage display technology as a selection-based system is an attractive method for evolution of new biological drugs. Unique ability of phage libraries for displaying proteins on bacteriophage surfaces enable them to make a major contribution in diverse fields of researches related to the diagnosis and therapy of diseases. One of the great challenges facing researchers is the modification of phage display technology and the development of new applications. This article reviews the molecular basis of phage display library, and summarizes the novel and specific applications of this technique in the field of biological drugs development including therapeutic antibodies, peptides, vaccines, and catalytic antibodies.

In the past decades, the mainstay of systemic therapy for solid and haematological malignancies was chemotherapy; nevertheless this modality has the drawbacks such as drug resistance and eliciting sever cytotoxicity in the normal tissue. To resolve such downsides, the cancer therapy modalities need to be advanced with more effective and tolerable treatments to specifically target the malignant cell with minimal adverse consequences. In fact, characteristically, the malignant diseases are self sufficiency in growth signals along with insensitivity to growth inhibition. They can also evade from apoptosis, have limitless replicative potential, induce angiogenesis and possess metastasis potential. Given that the most of these characteristics are often due to genetic defects, thus key to the development of targeted therapies is the ability to use such processes to phenotypically distinguish the tumor from its normal counterpart by its specific/selective markers. The therapeutic monoclonal antibodies (mAbs) are deemed to be a class of novel agents that can specifically target and disrupt molecular pathways underlying tumorigenesis. The mAbs are produced by a single clone of B-cells, and are monospecific and homogeneous. Since Kohler and Milstein heralded a new era in antibody research and clinical development by the discovery of hybridoma technology in 1975, more than 20 mAbs have been approved by the US Food and Drug Administration (FDA) for treatment of obdurate diseases, including different types of cancers. Mouse hybridomas were the first reliable source of monoclonal antibodies which were developed for several in vivo therapeutic applications. Accordingly, the recombinant antibodies have been reduced in size, rebuilt into multivalent molecules and fused with different moieties such as radionuclides, toxins and enzymes. The emergence of recombinant technologies, transgenic animals and phage display technology has revolutionized the selection, humanization and production of antibodies. This review focuses on implementation of the mAbs and nanobodies fragments for cancer therapy.