Evidence of conserved epitopes in variable region of VP8* subunit of VP4 protein of rotaviruses of P[8]-1 and P[8]-3 lineages.

نویسندگان

  • J F Contreras
  • G E Menchaca
  • R Infante
  • C E Hernández
  • C Rodríguez
  • R S Tamez
چکیده

Although antibody responses to the human rotavirus VP4 protein have been reported, few studies have analyzed the specificity of these responses to the VP8* subunit. This study investigated antibody responses generated against the variable region of the VP4 protein (VP8* subunit) in children infected with rotavirus genotype P[8]. Recombinant VP8* subunit (rVP8*) and truncations corresponding aa 1-102 (peptide A) and 84-180 (peptide B) of rotavirus strains P[8]-1 and P[8]-3 lineages were expressed in Escherichia coli and examined for antibody reactivity using ELISA and Western blot assays. Sera from infected children had IgG antibodies that reacted with full-length rVP8*, peptide A and B of both lineages, with stronger reactivity observed against peptide B. In addition, anti-strain Wa (P[8]-1) and anti-rVP8* (P[8]-3) rabbit polyclonal antiserum reacted against peptide B sequences of both lineages. These data indicate that the VP8* variable region of rotavirus belonging to P[8]-1 and P[8]-3 lineages have conserved epitopes recognized by antibodies elicited during natural infections.

برای دانلود 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

Passive protection against rotavirus-induced diarrhea by monoclonal antibodies to the heterotypic neutralization domain of VP7 and the VP8 fragment of VP4.

A murine model was used to determine whether neutralizing monoclonal antibodies (MAbs) with heterotypic specificity directed to VP7 (MAb 57-8) or to the VP8 fragment of VP4 (MAb M14) passively protect mice against challenge with various strains of rotavirus. (The gene 4 product, an outer capsid protein, has traditionally been called VP3. It has been proposed, however, that the rotavirus gene 4 ...

متن کامل

In silico Analysis of Pasteurella multocida PlpE Protein Epitopes As Novel Subunit Vaccine Candidates

Background: Pasteurella multocida is a Gram-negative, non-motile, non-spore forming, and aerobic/anaerobic cocobacillus known as the causative agent of human and animal diseases. Humans can often be affected by cat scratch or bite, which may lead to soft tissue infections and in rare cases to bacteremia and septicemia. Commercial vaccines against this agent include inactivated, live attenuated,...

متن کامل

Diversity of group A rotavirus genes detected in the Triângulo Mineiro region, Minas Gerais, Brazil

Group A rotaviruses are the main causative agent of infantile gastroenteritis. The segmented nature of the viral genome allows reassortment of genome segments, which can generate genetic variants. In this study, we characterized the diversity of the VP7, VP4 (VP8*), VP6, NSP4, and NSP5 genes of the rotaviruses that circulated from 2005 to 2011 in the Triângulo Mineiro (TM) region of Brazil. Sam...

متن کامل

VP4 differentially regulates TRAF2 signaling, disengaging JNK activation while directing NF-kappa B to effect rotavirus-specific cellular responses.

Rotaviruses rapidly activate NF-kappaB and induce the secretion of selected chemokines after infection. The ability of rotavirus particles lacking genomic RNA to activate NF-kappaB suggested that rotavirus proteins direct cell signaling responses. We identified conserved TNFR-associated factor (TRAF) binding motifs within the rotavirus capsid protein VP4 and its N-terminal VP8* cleavage product...

متن کامل

Relative roles of GM1 ganglioside, N-acylneuraminic acids, and α2β1 integrin in mediating rotavirus infection.

UNLABELLED N-acetyl- and N-glycolylneuraminic acids (Sia) and α2β1 integrin are frequently used by rotaviruses as cellular receptors through recognition by virion spike protein VP4. The VP4 subunit VP8*, derived from Wa rotavirus, binds the internal N-acetylneuraminic acid on ganglioside GM1. Wa infection is increased by enhanced internal Sia access following terminal Sia removal from main glyc...

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

برای دانلود 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

عنوان ژورنال:
  • Acta virologica

دوره 55 3  شماره 

صفحات  -

تاریخ انتشار 2011