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Human Vaccines: Emerging Technologies in Design and Development

Human Vaccines: Emerging Technologies in Design and Development

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Human Vaccines: Emerging Technologies in Design and Development

414 pagine
2 ore
Oct 15, 2016


Human Vaccines: Emerging Technologies in Design and Development discusses the advances in molecular biology, biophysics, and informatics—among other disciplines—that have provided scientists with the tools to create new vaccines against emerging and re-emerging pathogens.

For example, the virus-like particle technologies that led to licensing of highly efficacious HPV vaccines have only come into full realization in the last 10 years. Their success has, in turn, accelerated the pace with which nanoparticle vaccines are being developed

Given the rapidity with which the field is changing and the absence of any text documenting this change, there is a need for a resource that surveys these new vaccine technologies, assesses their potential, and describes their applications. This book provides that resource and complements traditional vaccinology books, but also serves as an excellent standalone for researchers and students with basic knowledge in immunology.

  • Introduces new topics in vaccine immunology in the context vaccine design and production
  • Consolidates the growing body of knowledge on new vaccine technologies that have only emerged in the past 2 – 3 decades
  • Reviews the currently licensed vaccines that have utilized leading-edge technologies and how this has translated into improved efficacy and safety
  • Provides a broad overview of innovative vaccine technologies, including immunological aspects
Oct 15, 2016

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Human Vaccines - Academic Press


Part I

Designing Vaccines From a New Starting Point


Chapter 1 Broadly Neutralizing Antibodies

Chapter 1

Broadly Neutralizing Antibodies

L. Morris¹ and T.A. Moody²,    ¹National Institute for Communicable Diseases, Johannesburg, South Africa,    ²Duke University, Durham, NC, United States


Effective vaccines for a number of human pathogens are lacking. In general, vaccines mimic natural protective immune responses. Thus, the improved ability to harness the native power of the human immune system and isolate pathogen-specific antibodies is helping to fill an important gap in vaccine development. Here we highlight the technological advances that have fast-tracked the discovery of new anti-infective monoclonal antibodies (mAbs). We discuss their role in a reverse vaccinology approach toward facilitating the design of better immunogens. We also review the development of mAbs as biological drugs to both prevent and treat infectious diseases. This chapter will focus mainly on human immunodeficiency virus type 1 and influenza virus but will also discuss other pathogens where significant progress has been made, as in the case of respiratory syncytial virus. These technologies are applicable across different diseases, providing a platform for tackling new or reemerging pathogens, such as Ebola viruses. The emergence and expansion of monoclonal antibody technologies herald a new era in the fight against infectious diseases.


Monoclonal antibodies; neutralization; single B cell sorting; B cell culture; high-throughput screening; next-generation sequencing; reverse vaccinology; human immunodeficiency virus; influenza

The antibody response to human pathogens is generally robust, highly specific, long-lasting and, in many cases, able to clear infection. The initial encounter between a naïve B cell receptor (BCR) and a foreign antigen activates B cell clonal lineages that subsequently undergo somatic hypermutation and selection in a process that increases antibody affinity. In most cases, the first detectable antibody response in the plasma is of the IgM class, switching to IgG and IgA classes within several weeks after infection. As most high-affinity antibodies develop, B cells engage CD4+ T follicular helper cells in germinal centers and exit as plasmablasts. Intermediate IgM and class-switched memory B cells are also released into circulation at predictable intervals during the process.¹,² Large quantities of antibodies are produced by short-lived plasmablasts that are found in the circulation during an acute infection. These cells appear in particularly high numbers in response to human immunodeficiency virus type 1 (HIV-1), although the vast majority are not HIV-1-specific because of extensive B cell hyperactivation that is a hallmark of the disease.³ For those infections that are cleared, resolution is associated with a decline in the circulating plasmablast and retention memory B cell pools that are available for recall upon subsequent exposures. Consequently, secondary responses are more rapid, generate higher affinity antibodies and mediate protection against reinfection or at least severe disease.

The BCR is an integral membrane form of the antibody that is specific to each B cell. Antibodies are heterodimeric proteins consisting of heavy and light chains that combine to form a basic Y shaped structure. Both surface-bound and secreted antibodies have a compartmentalized construction that includes a region able to recognize antigens. The process of antibody gene rearrangement⁴ results in a large array of antibody binding sites that are further diversified by somatic hypermutation.⁵ Each antibody contains two antigen recognition sites making up each arm of the Y shaped structure. These portions—the fragment antigen binding or Fab regions—are the primary focus of efforts to isolate and characterize human antibodies. The third major functional and structural component of an antibody is the fragment constant or Fc region that defines antibody isotypes and subclasses. It interacts with effector arms of the immune system either by binding receptor molecules (e.g., plasma complement proteins) or by binding cell surface receptors on effector cells (e.g., NK cells). These Fc-mediated effector functions likely play an important role in a number of infections as they enhance the antiviral efficacy of antibodies. Antibody functions can be further manipulated through recombinant engineering of the Fc region, either by mutating amino acid residues, changing glycosylation patterns, or both. This has been a common practice for the development of monoclonal antibodies (mAbs) in clinical

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