A Naturally Occurring Antibody Fragment Neutralizes Infectivity of Diverse Infectious Agents

نویسندگان

  • Luciano Polonelli
  • Tecla Ciociola
  • Lisa Elviri
  • Pier Paolo Zanello
  • Laura Giovati
  • Denise C. Arruda
  • Julián E. Muñoz
  • Renato A. Mortara
  • Giulia Morace
  • Elisa Borghi
  • Serena Galati
  • Oriano Marin
  • Claudio Casoli
  • Elisabetta Pilotti
  • Paola Ronzi
  • Luiz R. Travassos
  • Walter Magliani
  • Stefania Conti
چکیده

A phosphorylated peptide, named K40H, derived from the constant region of IgMs was detected in human serum by liquid chromatography coupled to high-resolution mass spectrometry. Synthetic K40H proved to exert a potent in vitro activity against fungal pathogens, and to inhibit HIV-1 replication in vitro and ex vivo. It also showed a therapeutic effect against an experimental infection by Candida albicans in the invertebrate model Galleria mellonella. K40H represents the proof of concept of the innate role that naturally occurring antibody fragments may exert against infectious agents, shedding a new light upon the posthumous role of antibodies and opening a new scenario on the multifaceted functionality of humoral immunity.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Naturally occurring antiglobulin factors in virus neutralization: homoreactant as a factor enhancing neutralization of the infectious complex of poliovirus with the Fab' antibody fragment.

A factor present in normal rabbit sera enhanced the neutralization of the infectious complex of poliovirus with the pepsin Fab' fragment of rabbit immunoglobulin G (IgG) antibody but showed no activity for the infectious complex of the same virus with IgG antibody. The factor was associated with IgG, and its activity was inhibited by the pepsin Fab' fragment of normal rabbit IgG. The data sugge...

متن کامل

A monoclonal antibody that neutralizes poliovirus by cross-linking virions.

The neutralization of type 1 poliovirus by monoclonal antibody 35-1f4 was studied. The virions were rapidly linked by antibody into oligomers and larger aggregates, followed by slow redistribution of antibody between the immune complexes. The antibody content and infectivity of immune complexes were determined. Remaining single virions were fully infectious and free of antibody. The oligomers a...

متن کامل

Entry of Ebola Virus is an Asynchronous Process.

Ebola virus (EBOV) is responsible for a severe fever with a high mortality rate. The diverse nature of the attachment of the virus to the cell surface, the initial step of virus entry, raises questions concerning the kinetics of the virus internalization process. We investigated EBOV entry kinetics using the activity of a particular monoclonal antibody that neutralizes virus infectivity. We dem...

متن کامل

Bovine Spongiform Encephalopathy Infectivity in Greater Kudu (Tragelaphus strepsiceros)

Of all the species exposed naturally to the bovine spongiform encephalopathy (BSE) agent, the greater kudu (Tragelaphus strepsiceros), a nondomesticated bovine from Africa, appears to be the most susceptible to the disease. We present the results of mouse bioassay studies to show that, contrary to findings in cattle with BSE in which the tissue distribution of infectivity is the most limited re...

متن کامل

Antibody to the 32K structural protein of infectious bursal disease virus neutralizes viral infectivity in vitro and confers protection on young chickens.

Chicken sera containing IgG antibodies specific for the 32 000 (32K) mol. wt. structural polypeptide of infectious bursal disease (IBD) virus, as assessed by Western blotting, neutralized the in vitro infectivity of tissue culture-adapted IBD virus. When injected into young chickens, the serum passively protected them from challenge with pathogenic IBD virus. Chickens immunized with the 32K str...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره 6  شماره 

صفحات  -

تاریخ انتشار 2016