Limits...
Phlebotomus papatasi SP15: mRNA expression variability and amino acid sequence polymorphisms of field populations.

Ramalho-Ortigão M, Coutinho-Abreu IV, Balbino VQ, Figueiredo CA, Mukbel R, Dayem H, Hanafi HA, El-Hossary SS, Fawaz Eel-D, Abo-Shehada M, Hoel DF, Stayback G, Wadsworth M, Shoue DA, Abrudan J, Lobo NF, Mahon AR, Emrich SJ, Kamhawi S, Collins FH, McDowell MA - Parasit Vectors (2015)

Bottom Line: The Phlebotomus papatasi salivary protein PpSP15 was shown to protect mice against Leishmania major, suggesting that incorporation of salivary molecules in multi-component vaccines may be a viable strategy for anti-Leishmania vaccines.In addition, predicted MHC class II T-cell epitopes were obtained and compared to areas of amino acid sequence variability within the secreted protein.The analysis of PpSP15 expression from field populations revealed significant intra- and interpopulation variation..

View Article: PubMed Central - PubMed

Affiliation: Department of Entomology, Kansas State University, Manhattan, KS, 66506, USA. mortigao@k-state.edu.

ABSTRACT

Background: The Phlebotomus papatasi salivary protein PpSP15 was shown to protect mice against Leishmania major, suggesting that incorporation of salivary molecules in multi-component vaccines may be a viable strategy for anti-Leishmania vaccines.

Methods: Here, we investigated PpSP15 predicted amino acid sequence variability and mRNA profile of P. papatasi field populations from the Middle East. In addition, predicted MHC class II T-cell epitopes were obtained and compared to areas of amino acid sequence variability within the secreted protein.

Results: The analysis of PpSP15 expression from field populations revealed significant intra- and interpopulation variation.. In spite of the variability detected for P. papatasi populations, common epitopes for MHC class II binding are still present and may potentially be used to boost the response against Le. major infections.

Conclusions: Conserved epitopes of PpSP15 could potentially be used in the development of a salivary gland antigen-based vaccine.

No MeSH data available.


Related in: MedlinePlus

PpSP15 polymorphisms. The predicted PpSP15 mature amino acid sequence is shown (based on sequence accession # AAL11047). Lower case characters represent singletons (unique polymorphic sites) identified in this study; In bold are shared polymorphic sites found in our analyses; bold and underlined are polymorphic sites present in our analyses and also identified by [12];black box characters represent shared polymorphisms found only by [12]. Yellow, gray and white background segments represent alpha helices, beta sheets and coil, according to secondary structure prediction. Regions of PpSP15 displaying predicted MHC class II peptides are boxed
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
getmorefigures.php?uid=PMC4472253&req=5

Fig5: PpSP15 polymorphisms. The predicted PpSP15 mature amino acid sequence is shown (based on sequence accession # AAL11047). Lower case characters represent singletons (unique polymorphic sites) identified in this study; In bold are shared polymorphic sites found in our analyses; bold and underlined are polymorphic sites present in our analyses and also identified by [12];black box characters represent shared polymorphisms found only by [12]. Yellow, gray and white background segments represent alpha helices, beta sheets and coil, according to secondary structure prediction. Regions of PpSP15 displaying predicted MHC class II peptides are boxed

Mentions: Multiple promiscuous MHC class II epitopes were identified using the three predictive software tools (Fig. 5). Using the threshold setting of 3 (on a scale 1-to-10, 1 = most stringent; 10 = least stringent), the number of predicted epitopes varied according to HLA allele, ranging from none predicted (such as in the case of alleles DRB1_ 1104, DRB1_ 1106, and DRB1_ 1311) to as many as 7 predicted binding peptides (as in the case of alleles DRB1_0305, DRB1_0306, DRB1_0307, and DRB1_0311). The majority of the predicted MHC class II binding sites (17 out of 22 epitopes from 67 alleles) were localized between the isoleucine residue at position 43 (I43) and the glutamine at position 107 (Q107) in the secreted PpSP15 sequence. Many of the binding sites in this region of the protein are overlapping. Four of the MHC class II epitopes predicted were found between tyrosine 28 (Y28) and alanine 39 (A39), and a single predicted MHC class II epitope was predicted between phenylalanine 11 (F11) and alanine 19 (A19).Fig. 5


Phlebotomus papatasi SP15: mRNA expression variability and amino acid sequence polymorphisms of field populations.

Ramalho-Ortigão M, Coutinho-Abreu IV, Balbino VQ, Figueiredo CA, Mukbel R, Dayem H, Hanafi HA, El-Hossary SS, Fawaz Eel-D, Abo-Shehada M, Hoel DF, Stayback G, Wadsworth M, Shoue DA, Abrudan J, Lobo NF, Mahon AR, Emrich SJ, Kamhawi S, Collins FH, McDowell MA - Parasit Vectors (2015)

PpSP15 polymorphisms. The predicted PpSP15 mature amino acid sequence is shown (based on sequence accession # AAL11047). Lower case characters represent singletons (unique polymorphic sites) identified in this study; In bold are shared polymorphic sites found in our analyses; bold and underlined are polymorphic sites present in our analyses and also identified by [12];black box characters represent shared polymorphisms found only by [12]. Yellow, gray and white background segments represent alpha helices, beta sheets and coil, according to secondary structure prediction. Regions of PpSP15 displaying predicted MHC class II peptides are boxed
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4472253&req=5

Fig5: PpSP15 polymorphisms. The predicted PpSP15 mature amino acid sequence is shown (based on sequence accession # AAL11047). Lower case characters represent singletons (unique polymorphic sites) identified in this study; In bold are shared polymorphic sites found in our analyses; bold and underlined are polymorphic sites present in our analyses and also identified by [12];black box characters represent shared polymorphisms found only by [12]. Yellow, gray and white background segments represent alpha helices, beta sheets and coil, according to secondary structure prediction. Regions of PpSP15 displaying predicted MHC class II peptides are boxed
Mentions: Multiple promiscuous MHC class II epitopes were identified using the three predictive software tools (Fig. 5). Using the threshold setting of 3 (on a scale 1-to-10, 1 = most stringent; 10 = least stringent), the number of predicted epitopes varied according to HLA allele, ranging from none predicted (such as in the case of alleles DRB1_ 1104, DRB1_ 1106, and DRB1_ 1311) to as many as 7 predicted binding peptides (as in the case of alleles DRB1_0305, DRB1_0306, DRB1_0307, and DRB1_0311). The majority of the predicted MHC class II binding sites (17 out of 22 epitopes from 67 alleles) were localized between the isoleucine residue at position 43 (I43) and the glutamine at position 107 (Q107) in the secreted PpSP15 sequence. Many of the binding sites in this region of the protein are overlapping. Four of the MHC class II epitopes predicted were found between tyrosine 28 (Y28) and alanine 39 (A39), and a single predicted MHC class II epitope was predicted between phenylalanine 11 (F11) and alanine 19 (A19).Fig. 5

Bottom Line: The Phlebotomus papatasi salivary protein PpSP15 was shown to protect mice against Leishmania major, suggesting that incorporation of salivary molecules in multi-component vaccines may be a viable strategy for anti-Leishmania vaccines.In addition, predicted MHC class II T-cell epitopes were obtained and compared to areas of amino acid sequence variability within the secreted protein.The analysis of PpSP15 expression from field populations revealed significant intra- and interpopulation variation..

View Article: PubMed Central - PubMed

Affiliation: Department of Entomology, Kansas State University, Manhattan, KS, 66506, USA. mortigao@k-state.edu.

ABSTRACT

Background: The Phlebotomus papatasi salivary protein PpSP15 was shown to protect mice against Leishmania major, suggesting that incorporation of salivary molecules in multi-component vaccines may be a viable strategy for anti-Leishmania vaccines.

Methods: Here, we investigated PpSP15 predicted amino acid sequence variability and mRNA profile of P. papatasi field populations from the Middle East. In addition, predicted MHC class II T-cell epitopes were obtained and compared to areas of amino acid sequence variability within the secreted protein.

Results: The analysis of PpSP15 expression from field populations revealed significant intra- and interpopulation variation.. In spite of the variability detected for P. papatasi populations, common epitopes for MHC class II binding are still present and may potentially be used to boost the response against Le. major infections.

Conclusions: Conserved epitopes of PpSP15 could potentially be used in the development of a salivary gland antigen-based vaccine.

No MeSH data available.


Related in: MedlinePlus